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30 results on '"MESH : Sequence Alignment"'

1. Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system from Porphyromonas gingivalis

Author

Christian Cambillau, Christine Kellenberger, Alain Roussel, Aline Desmyter, Anaïs Gaubert, Jennifer Roche, Philippe Leone, Thi Trang Nhung Trinh, Yoan Duhoo, Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Architecture et fonction des macromolécules biologiques ( AFMB ), and Centre National de la Recherche Scientifique ( CNRS ) -Aix Marseille Université ( AMU ) -Institut National de la Recherche Agronomique ( INRA )

Subjects
MESH: Sequence Homology, Amino Acid, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Plasma protein binding, MESH: Amino Acid Sequence, Biochemistry, MESH: Recombinant Proteins, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH: Animals, [ SDV.BIBS ] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Peptide sequence, MESH: Bacterial Proteins, MESH : Porphyromonas gingivalis, MESH : Protein Conformation, alpha-Helical, [SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases, [ SDV.MHEP.ME ] Life Sciences [q-bio]/Human health and pathology/Emerging diseases, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Escherichia coli, MESH : Amino Acid Sequence, MESH : Protein Binding, MESH: Camelus, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], MESH : Sequence Homology, Amino Acid, MESH : Genetic Vectors, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [ SDV.MHEP.MI ] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH : Crystallization, [ SDV.NEU.NB ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Camelids, New World, MESH: Porphyromonas gingivalis, MESH: Models, Molecular, Camelus, MESH: Gene Expression, MESH : Cloning, Molecular, Biophysics, MESH: Sequence Alignment, [ SDV.MP.VIR ] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Single-Domain Antibodies, Microbiology, 03 medical and health sciences, Bacterial Proteins, Genetics, MESH: Protein Binding, Secretion, Molecular replacement, Protein Interaction Domains and Motifs, 5fwo, MESH: Cloning, Molecular, Amino Acid Sequence, Porphyromonas gingivalis, MESH: Protein Conformation, alpha-Helical, [ SDV.IMM.II ] Life Sciences [q-bio]/Immunology/Innate immunity, MESH: Protein Interaction Domains and Motifs, MESH : Molecular Chaperones, Periplasmic space, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH : Camelids, New World, MESH : Gene Expression, 030104 developmental biology, MESH: Binding Sites, Protein Conformation, beta-Strand, PorM, Molecular Chaperones, type IX secretion system, 0301 basic medicine, Models, Molecular, Protein Conformation, alpha-Helical, MESH : Escherichia coli, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, Gene Expression, [ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Crystallography, X-Ray, [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity, MESH : Bacterial Secretion Systems, Research Communications, [ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Structural Biology, MESH: Genetic Vectors, 5lmj, MESH : Bacterial Proteins, Cloning, Molecular, MESH: Bacterial Secretion Systems, Bacterial Secretion Systems, MESH : Protein Conformation, beta-Strand, MESH: Crystallization, 5lmw, MESH: Kinetics, MESH : Sequence Alignment, MESH : Camelus, Condensed Matter Physics, Recombinant Proteins, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], MESH : Single-Domain Antibodies, Thermodynamics, MESH: Protein Conformation, beta-Strand, nb02, MESH : Kinetics, nb01, MESH: Thermodynamics, MESH: Molecular Chaperones, Crystallization, Camelids, New World, Protein Binding, crystallization chaperones, MESH : Recombinant Proteins, MESH : Models, Molecular, Genetic Vectors, Context (language use), Biology, MESH : Peptide Library, Peptide Library, Escherichia coli, Animals, nb130, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Peptide library, MESH : Thermodynamics, nb19, Binding Sites, Sequence Homology, Amino Acid, [ SDV.SP.PHARMA ] Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, [ SDV.BIO ] Life Sciences [q-bio]/Biotechnology, Single-Domain Antibodies, biology.organism_classification, MESH: Crystallography, X-Ray, Kinetics, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH : Animals, MESH: Peptide Library, MESH : Crystallography, X-Ray, camelid nanobodies, Sequence Alignment, 5lz0, MESH : Binding Sites, MESH : Protein Interaction Domains and Motifs, [ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract

PorM is a membrane protein that is involved in the assembly of the type IX secretion system (T9SS) inPorphyromonas gingivalis, a major bacterial pathogen that is responsible for periodontal disease in humans. In the context of structural studies of PorM to better understand T9SS assembly, four camelid nanobodies were selected, produced and purified, and their specific interaction with the N-terminal or C-terminal part of the periplasmic domain of PorM was investigated. Diffracting crystals were also obtained, and the structures of the four nanobodies were solved by molecular replacement. Furthermore, two nanobodies were used as crystallization chaperones and turned out to be valuable tools in the structure-determination process of the periplasmic domain of PorM.

Published
2017
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2. Characterization of Unique Signature Sequences in the Divergent Maternal Protein Bcl2l10

Author

Germain Gillet, Abdel Aouacheria, François Penin, Aurélie Cornut-Thibaut, Yannis Guillemin, Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Ganivet, Agnès, Institut de biologie et chimie des protéines [Lyon] ( IBCP ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Centre de Recherche en Cancérologie de Lyon ( CRCL ), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie Moléculaire de la Cellule ( LBMC ), École normale supérieure - Lyon ( ENS Lyon ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), and École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL)

Subjects
MESH : Cell Line, MESH : Molecular Sequence Data, Amino Acid Motifs, MESH: Amino Acid Sequence, MESH: Base Sequence, MESH : Proto-Oncogene Proteins c-bcl-2, [ SDV.CAN ] Life Sciences [q-bio]/Cancer, MESH: INDEL Mutation, protein sequence, MESH: Amino Acid Motifs, MESH: Protein Structure, Tertiary, 0302 clinical medicine, INDEL Mutation, Databases, Genetic, genetic polymorphism, MESH : Female, MESH: Animals, MESH: Genetic Variation, [SDV.BDD]Life Sciences [q-bio]/Development Biology, Peptide sequence, MESH: Databases, Genetic, MESH: Evolution, Molecular, Sequence Deletion, Genetics, chemistry.chemical_classification, 0303 health sciences, MESH : Amino Acid Sequence, MESH : Sequence Alignment, apoptosis, Vertebrate, MESH: Sequence Deletion, Amino acid, Proto-Oncogene Proteins c-bcl-2, MESH: Calcium, 030220 oncology & carcinogenesis, Female, MESH : Protein Structure, Tertiary, MESH : Amino Acid Motifs, Molecular Sequence Data, MESH: Sequence Alignment, [SDV.CAN]Life Sciences [q-bio]/Cancer, Sequence alignment, Biology, Cell Line, MESH: Oocytes, Evolution, Molecular, 03 medical and health sciences, Bcl-2 family, MESH : Genetic Variation, biology.animal, evolution, [SDV.BDD] Life Sciences [q-bio]/Development Biology, Genetic variation, Homologous chromosome, Animals, Humans, MESH : HeLa Cells, MESH : Evolution, Molecular, Amino Acid Sequence, MESH : Calcium, MESH : Databases, Genetic, Indel, MESH : INDEL Mutation, Molecular Biology, Ecology, Evolution, Behavior and Systematics, 030304 developmental biology, MESH : Mutagenesis, Insertional, calcium, MESH: Humans, MESH: Molecular Sequence Data, Base Sequence, MESH : Sequence Deletion, MESH: Apoptosis, MESH : Humans, MESH : Oocytes, Genetic Variation, Protein Structure, Tertiary, MESH: Cell Line, Mutagenesis, Insertional, MESH: Mutagenesis, Insertional, MESH: Proto-Oncogene Proteins c-bcl-2, chemistry, MESH: HeLa Cells, Oocytes, MESH : Base Sequence, MESH : Animals, Sequence Alignment, MESH: Female, MESH : Apoptosis, HeLa Cells
Abstract

International audience; Insertions or deletions (indels) of amino acids residues have been recognized as an important source of genetic and structural divergence between paralogous Bcl-2 family members. However, these signature sequences have not so far been extensively investigated amongst orthologous Bcl-2 family proteins. Bcl2l10 is an antiapoptotic member of the Bcl-2 family that has evolved rapidly throughout the vertebrate lineage and which shows conserved abundant expression in eggs and oocytes. In this paper, we have unraveled two major sites of divergence between human Bcl2l10 and its vertebrate homologs. The first one provides length variation at the N-terminus (before the BH4 domain) and the second one is located between the predicted α5-α6 pore-forming helices, providing an unprecedented case in the superfamily of helix-bundled pore-forming proteins. These two particular indels were studied phylogenetically and through biochemical and cell biological techniques, including truncation and site-directed mutagenesis. While deletion of the N-terminal extension had no significant functional impact in HeLa cells, our results suggest that the human Bcl2l10 protein evolved a calcium-binding motif in its α5-α6 interhelical region by acquiring critical negatively charged residues. Considering the reliance of female eggs on calcium-dependent proteins and calcium-regulated processes and the exceptional longevity of oocytes in the primate lineage, we propose that this microstructural variation may be an adaptive feature associated with high maternal expression of this Bcl-2 family member.

Published
2011
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3. Functional characterization of the AFF (AF4/FMR2) family of RNA-binding proteins: insights into the molecular pathology of FRAXE intellectual disability

Author

Mireille Melko, Samantha Zongaro, Jozef Gecz, Dominique Douguet, Barbara Bardoni, Céline Verheggen, Mounia Bensaid, Institut de pharmacologie moléculaire et cellulaire ( IPMC ), Université Nice Sophia Antipolis ( UNS ), Université Côte d'Azur ( UCA ) -Université Côte d'Azur ( UCA ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Centre National de la Recherche Scientifique ( CNRS ) -Université de Montpellier ( UM ), Department of Genetic Medicine Women's and Children's, University of Adelaide, Université Côte d'Azur ( UCA ), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)

Subjects
MESH : Cell Line, MESH : Molecular Sequence Data, MESH: Sequence Homology, Amino Acid, Gene Expression, RNA-binding protein, MESH: Amino Acid Sequence, MESH: Gene Order, Exon, 0302 clinical medicine, MESH : Protein Transport, Genes, Reporter, Transcription (biology), Gene Order, Genetics (clinical), Genetics, 0303 health sciences, MESH : Amino Acid Sequence, MESH : Sequence Alignment, RNA-Binding Proteins, General Medicine, MESH : Genes, Reporter, Phenotype, MESH : Sequence Homology, Amino Acid, DNA-Binding Proteins, Protein Transport, MESH : Fragile X Syndrome, 030220 oncology & carcinogenesis, RNA splicing, MESH : RNA Splicing, MESH : DNA-Binding Proteins, Intranuclear Space, MESH: Fragile X Syndrome, MESH: Protein Transport, MESH: Gene Expression, RNA Splicing, Molecular Sequence Data, MESH : RNA-Binding Proteins, MESH: Sequence Alignment, MESH: Intranuclear Space, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Cell Line, 03 medical and health sciences, MESH : Fibroblasts, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : HeLa Cells, Amino Acid Sequence, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, Gene, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Humans, MESH : Gene Order, Sequence Homology, Amino Acid, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH: Genes, Reporter, MESH : Humans, Alternative splicing, RNA, Fibroblasts, MESH: Cell Line, MESH : Gene Expression, MESH: RNA-Binding Proteins, MESH : Intranuclear Space, MESH: Fibroblasts, Fragile X Syndrome, MESH: HeLa Cells, MESH: RNA Splicing, Sequence Alignment, MESH: DNA-Binding Proteins, HeLa Cells
Abstract

International audience; The AFF (AF4/FMR2) family of genes includes four members: AFF1/AF4, AFF2/FMR2, AFF3/LAF4 and AFF4/AF5q31. AFF2/FMR2 is silenced in FRAXE intellectual disability, while the other three members have been reported to form fusion genes as a consequence of chromosome translocations with the myeloid/lymphoid or mixed lineage leukemia (MLL) gene in acute lymphoblastic leukemias (ALLs). All AFF proteins are localized in the nucleus and their role as transcriptional activators with a positive action on RNA elongation was primarily studied. We have recently shown that AFF2/FMR2 localizes to nuclear speckles, subnuclear structures considered as storage/modification sites of pre-mRNA splicing factors, and modulates alternative splicing via the interaction with the G-quadruplex RNA-forming structure. We show here that similarly to AFF2/FMR2, AFF3/LAF4 and AFF4/AF5q31 localize to nuclear speckles and are able to bind RNA, having a high apparent affinity for the G-quadruplex structure. Interestingly, AFF3/LAF4 and AFF4/AF5q31, like AFF2/FMR2, modulate, in vivo, the splicing efficiency of a mini-gene containing a G-quadruplex structure in one alternatively spliced exon. Furthermore, we observed that the overexpression of AFF2/3/4 interferes with the organization and/or biogenesis of nuclear speckles. These findings fit well with our observation that enlarged nuclear speckles are present in FRAXE fibroblasts. Furthermore, our findings suggest functional redundancy among the AFF family members in the regulation of splicing and transcription. It is possible that other members of the AFF family compensate for the loss of AFF2/FMR2 activity and as such explain the relatively mild to borderline phenotype observed in FRAXE patients.

Published
2011
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4. Association of Microsatellite Variations of Plasmodium falciparum Na+/H+ Exchanger (Pfnhe-1) Gene with Reduced In Vitro Susceptibility to Quinine: Lack of Confirmation in Clinical Isolates from Africa

Author

Didier Menard, Christiane Bouchier, Jacques Le Bras, Rémy Durand, Véronique Hubert, Stéphane Rabearimanana, Magali Tichit, Valérie Andriantsoanirina, Institut Pasteur de Madagascar, Réseau International des Instituts Pasteur (RIIP), Immunologie moléculaire des parasites, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Centre National de Référence du Paludisme, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-AP-HP - Hôpital Bichat - Claude Bernard [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5), Génomique (Plate-Forme) - Genomics Platform, Institut Pasteur [Paris], Service de Parasitologie [Avicenne], Université Paris 13 (UP13)-Hôpital Avicenne [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP), Université Paris 13 (UP13)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Avicenne [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut Pasteur de Madagascar - Réseau International des Instituts Pasteur (RIIP), Institut Pasteur [Paris] - Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP) - AP-HP - Hôpital Bichat - Claude Bernard [Paris] - Université Paris Descartes - Paris 5 (UPD5), Génomique (Plate-Forme), Assistance publique - Hôpitaux de Paris (AP-HP) - Hôpital Avicenne - Université Paris 13 (UP13), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-AP-HP - Hôpital Bichat - Claude Bernard [Paris]-Université Paris Descartes - Paris 5 (UPD5), and Université Paris 13 (UP13)-Hôpital Avicenne-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)

Subjects
MESH : Molecular Sequence Data, MESH : Polymorphism, Genetic, Drug Resistance, Protozoan Proteins, MESH : Genotype, MESH: Amino Acid Sequence, MESH: Africa, MESH : Microsatellite Repeats, MESH : Malaria, Falciparum, MESH: Genotype, 0302 clinical medicine, MESH : Chloroquine, MESH : Quinine, Polymorphism (computer science), Genotype, MESH : Plasmodium falciparum, MESH: Animals, Malaria, Falciparum, MESH: Protozoan Proteins, MESH: Plasmodium falciparum, MESH: Inhibitory Concentration 50, Genetics, 0303 health sciences, Quinine, biology, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH: Malaria, Falciparum, Chloroquine, Articles, MESH: Chloroquine, MESH : Sodium-Hydrogen Antiporter, 3. Good health, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Infectious Diseases, MESH : Inhibitory Concentration 50, MESH: Drug Resistance, Microsatellite, medicine.drug, Sodium-Hydrogen Exchangers, MESH: Quinine, MESH : Africa, Molecular Sequence Data, Plasmodium falciparum, 030231 tropical medicine, MESH: Sequence Alignment, Antimalarials, Inhibitory Concentration 50, 03 medical and health sciences, Virology, MESH: Polymorphism, Genetic, parasitic diseases, Genetic variation, medicine, Animals, Humans, Amino Acid Sequence, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, Genotyping, MESH : Protozoan Proteins, MESH : Drug Resistance, Polymorphism, Genetic, MESH: Molecular Sequence Data, MESH: Sodium-Hydrogen Antiporter, MESH: Humans, 030306 microbiology, MESH : Humans, biology.organism_classification, MESH: Antimalarials, Genetic marker, Africa, MESH : Antimalarials, Parasitology, MESH : Animals, MESH: Microsatellite Repeats, Sequence Alignment, Microsatellite Repeats
Abstract

International audience; We sought to test the association of polymorphisms in Plasmodium falciparum nhe-1 (Pfnhe-1, gene PF13_0019) with in vitro susceptibility to quinine, which was previously reported in a limited number of reference strains or culture-adapted isolates. Determination of in vitro susceptibility to quinine, genotyping of Pfnhe-1 ms4760 microsatellite and polymorphism in codon 76 of Pfcrt were performed for 83 isolates obtained from symptomatic malaria-infected travelers returning from various African countries to France or from subjects living in Madagascar. Nineteen different ms4760 microsatellite profiles of Pfnhe-1 were found including 14 not previously described. Multivariate analysis showed no significant association between the in vitro susceptibility to quinine with particular ms4760 profiles. Contrary to previous reports, we only observed that the number of NHNDNHNNDDD repeats was positively associated with the increased IC50 of QN (P = 0.01). We concluded that the studied polymorphisms in Pfnhe-1 did not appear as valid molecular markers of in vitro susceptibility to quinine in P. falciparum isolates from Africa. Because we did not include any isolate of Asian origin in our series, these results did not exclude the possibility of regional associations, for example in South-East Asia.

Published
2010
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5. Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components

Author

Luc Ponchon, Alexis Huet, Madalena Renouard, Cécile Breyton, Rudi Lurz, Pascale Boulanger, Fabrice Confalonieri, Alan R. Davidson, Mohamed Chami, Yvan Zivanovic, Ali Flayhan, Paulette Decottignies, Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre d'études et de recherche en informatique et communications (CEDRIC), Ecole Nationale Supérieure d'Informatique pour l'Industrie et l'Entreprise (ENSIIE)-Conservatoire National des Arts et Métiers [CNAM] (CNAM), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire pour l'utilisation du rayonnement électromagnétique (LURE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-MENRT-Centre National de la Recherche Scientifique (CNRS), Muséum national d'Histoire naturelle (MNHN), Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Laboratoire de Réactivité de Surface (LRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Institut de génétique et microbiologie [Orsay] ( IGM ), Université Paris-Sud - Paris 11 ( UP11 ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de cristallographie et RMN biologiques ( LCRB - UMR 8015 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Centre d'étude et de recherche en informatique et communications ( CEDRIC ), Ecole Nationale Supérieure d'Informatique pour l'Industrie et l'Entreprise ( ENSIIE ) -Conservatoire National des Arts et Métiers [CNAM] ( CNAM ), Institut de biologie structurale ( IBS - UMR 5075 ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ) -Université Joseph Fourier - Grenoble 1 ( UJF ), Laboratoire pour l'utilisation du rayonnement électromagnétique ( LURE ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -MENRT-Centre National de la Recherche Scientifique ( CNRS ), Muséum National d'Histoire Naturelle ( MNHN ), Institut de biochimie et biophysique moléculaire et cellulaire ( IBBMC ), Laboratoire de Réactivité de Surface ( LRS ), and Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH : Escherichia coli, MESH : Molecular Sequence Data, viruses, MESH: Amino Acid Sequence, Siphoviridae, Genome, chemistry.chemical_compound, MESH: Capsid, Bacteriophages, MESH : Viral Proteins, Bacteriophage T5, MESH : Siphoviridae, 0303 health sciences, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Escherichia coli, MESH : Amino Acid Sequence, MESH : Sequence Alignment, 030302 biochemistry & molecular biology, MESH : Bacteriophages, Cell biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Capsid, Lytic cycle, MESH : Capsid, Molecular Sequence Data, Immunology, MESH: Sequence Alignment, MESH: Microscopy, Electron, Microbiology, Viral Proteins, 03 medical and health sciences, Virology, Escherichia coli, MESH: Siphoviridae, Amino Acid Sequence, MESH: Bacteriophages, Gene, 030304 developmental biology, MESH: Molecular Sequence Data, Structure and Assembly, biology.organism_classification, Molecular biology, MESH: Viral Proteins, MESH : Microscopy, Electron, Microscopy, Electron, chemistry, Cytoplasm, Insect Science, Sequence Alignment, DNA, [ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract

Bacteriophage T5 represents a large family of lytic Siphoviridae infecting Gram-negative bacteria. The low-resolution structure of T5 showed the T=13 geometry of the capsid and the unusual trimeric organization of the tail tube, and the assembly pathway of the capsid was established. Although major structural proteins of T5 have been identified in these studies, most of the genes encoding the morphogenesis proteins remained to be identified. Here, we combine a proteomic analysis of T5 particles with a bioinformatic study and electron microscopic immunolocalization to assign function to the genes encoding the structural proteins, the packaging proteins, and other nonstructural components required for T5 assembly. A head maturation protease that likely accounts for the cleavage of the different capsid proteins is identified. Two other proteins involved in capsid maturation add originality to the T5 capsid assembly mechanism: the single head-to-tail joining protein, which closes the T5 capsid after DNA packaging, and the nicking endonuclease responsible for the single-strand interruptions in the T5 genome. We localize most of the tail proteins that were hitherto uncharacterized and provide a detailed description of the tail tip composition. Our findings highlight novel variations of viral assembly strategies and of virion particle architecture. They further recommend T5 for exploring phage structure and assembly and for deciphering conformational rearrangements that accompany DNA transfer from the capsid to the host cytoplasm.

Published
2014
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6. Alternatives to carbapenems in ESBL-producing Escherichia coli infections

Author

Patrick Plésiat, Daniel Talon, Pascal Cholley, Xavier Bertrand, J. Leroy, Damien Fournier, Catherine Chirouze, Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon), Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Service des maladies infectieuses et tropicales, Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)-Hôpital Saint-Jacques, Hôpital Jean Minjoz, Centre Hospitalier Régional Universitaire [Besançon] ( CHRU Besançon ), Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), and Centre Hospitalier Régional Universitaire [Besançon] ( CHRU Besançon ) -Hôpital Saint-Jacques

Subjects
MESH : Escherichia coli, Cefotaxime, Ceftazidime, MESH: beta-Lactamases, MESH : Carbapenems, MESH: Escherichia coli Proteins, Tigecycline, Aztreonam, MESH: Carbapenems, chemistry.chemical_compound, 0302 clinical medicine, [ SDV.MP ] Life Sciences [q-bio]/Microbiology and Parasitology, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Drug Resistance, Multiple, Bacterial, polycyclic compounds, MESH : DNA, Bacterial, Temocillin, 030212 general & internal medicine, MESH : Anti-Bacterial Agents, Escherichia coli Infections, 0303 health sciences, MESH: Microbial Sensitivity Tests, MESH: Escherichia coli, Escherichia coli Proteins, MESH : Sequence Alignment, MESH : Escherichia coli Proteins, MESH : beta-Lactamases, [ SDV.SPEE ] Life Sciences [q-bio]/Santé publique et épidémiologie, Anti-Bacterial Agents, 3. Good health, [ SDV.MHEP.MI ] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Infectious Diseases, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, MESH : Escherichia coli Infections, MESH: Membrane Proteins, medicine.drug, DNA, Bacterial, MESH : Drug Resistance, Multiple, Bacterial, MESH: Sequence Alignment, Microbial Sensitivity Tests, Fosfomycin, Biology, MESH: Sequence Homology, Nucleic Acid, beta-Lactam Resistance, beta-Lactamases, Microbiology, 03 medical and health sciences, MESH : beta-Lactam Resistance, Sequence Homology, Nucleic Acid, MESH: Anti-Bacterial Agents, Escherichia coli, medicine, Humans, MESH : Sequence Homology, Nucleic Acid, Mecillinam, MESH: Escherichia coli Infections, MESH: Humans, 030306 microbiology, MESH : Humans, Membrane Proteins, MESH: Drug Resistance, Multiple, Bacterial, biochemical phenomena, metabolism, and nutrition, bacterial infections and mycoses, MESH: DNA, Bacterial, MESH: beta-Lactam Resistance, Carbapenems, chemistry, Nitrofurantoin, MESH : Membrane Proteins, bacteria, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, MESH : Microbial Sensitivity Tests, Sequence Alignment
Abstract

International audience; OBJECTIVES: The authors had for objective to assess the activity of a wide panel of antibiotics on extended-spectrum-β-lactamase producing Escherichia coli isolates (ESBL-Ec), because of the sharp increase of their frequency, leading to an increased use of carbapenems. MATERIAL AND METHODS: We selected 100 ESBL-Ec in which ESBLs were identified by PCR and sequencing, between 2009 and 2010. We determined the MICs of amoxicillin-clavulanate, piperacillin-tazobactam, temocillin, mecillinam, cefoxitin, cefotaxime, ceftazidime, aztreonam, tigecycline, nitrofurantoin, and fosfomycin using reference methods. The susceptibility profiles were defined according to EUCAST 2012 recommendations. RESULTS: Fosfomycin, nitrofurantoin, and pivmecillinam were active against more than 90% of isolates and remain excellent choices for the oral treatment of urinary tract infections (UTIs). Temocillin and piperacillin-tazobactam are also good candidates for the treatment of pyelonephritis or bloodstream infections. Only 27, 23, and 8% of isolates were susceptible to ceftazidime, cefepime, and cefotaxime, respectively. CONCLUSION: Our study results prove that in many cases, there are non-carbapenem alternatives for the treatment of ESBL-Ec infections.

Published
2013
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7. Ex vivo and in vivo inhibition of human rhinovirus replication by a new pseudosubstrate of viral 2A protease

Author

Fatma Berri, Bruno Lina, Didier Decimo, Jean-Claude Cortay, Sébastien Violot, Isabelle Schuffenecker, Béatrice Riteau, Florence Morfin, Théophile Ohlmann, Marie-Laure Foucault-Grunenwald, Nisrine Falah, Virologie et pathologie humaine (VirPath), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Virologie humaine, École normale supérieure - Lyon (ENS Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de Biologie et Pathologie Est, Bron, Laboratory of Virology East, Hospices Civils de Lyon (HCL), Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), National Reference Center of Enteroviruses, Institut de Veille Sanitaire, Agence Nationale de la Recherche (ANR), Virologie et pathologie humaine ( VirPath ), Université Claude Bernard Lyon 1 ( UCBL ), Laboratoire de physiologie cellulaire végétale ( LPCV ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut National de la Recherche Agronomique ( INRA ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), École normale supérieure - Lyon ( ENS Lyon ) -IFR128-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Hospices Civils de Lyon ( HCL ), École normale supérieure de Lyon (ENS de Lyon)-IFR128-Institut National de la Santé et de la Recherche Médicale (INSERM), and Centre de Biologie et Pathologie Est [Bron] (CBPE)

Subjects
MESH : Molecular Sequence Data, Rhinovirus, AIRWAY INFLAMMATION, medicine.medical_treatment, [SDV]Life Sciences [q-bio], Peptide, POLIOVIRUS, MESH: Amino Acid Sequence, medicine.disease_cause, Virus Replication, MESH: Down-Regulation, Substrate Specificity, MESH : Down-Regulation, Mice, MESH: Picornaviridae Infections, MESH : Female, MESH: Animals, MESH : Viral Proteins, Peptide sequence, chemistry.chemical_classification, MESH : Picornaviridae Infections, 0303 health sciences, Mice, Inbred BALB C, MESH: Rhinovirus, MESH : Substrate Specificity, MESH : Peptides, MESH: Peptides, MESH : Amino Acid Sequence, MESH : Sequence Alignment, 030302 biochemistry & molecular biology, MESH : Protein Binding, PEPTIDES, Cysteine protease, 3. Good health, MESH : Rhinovirus, MESH : Virus Replication, Cysteine Endopeptidases, INFECTIONS, MESH : Cysteine Endopeptidases, Female, Protein Binding, Immunology, Molecular Sequence Data, MESH: Mice, Inbred BALB C, MESH: Sequence Alignment, Down-Regulation, Biology, Microbiology, 03 medical and health sciences, Viral Proteins, In vivo, Virology, Vaccines and Antiviral Agents, MESH : Mice, medicine, Animals, Humans, MESH: Protein Binding, Amino Acid Sequence, MESH: Mice, MESH : Mice, Inbred BALB C, 030304 developmental biology, Protease, Picornaviridae Infections, MESH: Humans, MESH: Molecular Sequence Data, [ SDV ] Life Sciences [q-bio], STABILITY, CLEAVAGE, PROTEINASES, MESH : Humans, COXSACKIEVIRUS, MESH: Virus Replication, MESH: Viral Proteins, Viral replication, chemistry, Insect Science, RNA, MESH: Substrate Specificity, MESH : Animals, TRANSLATION, Sequence Alignment, MESH: Female, Ex vivo, MESH: Cysteine Endopeptidases
Abstract

Human rhinoviruses (HRVs) remain a significant public health problem as they are the major cause of both upper and lower respiratory tract infections. Unfortunately, to date no vaccine or antiviral against these pathogens is available. Here, using a high-throughput yeast two-hybrid screening, we identified a 6-amino-acid hit peptide, LVLQTM, which acted as a pseudosubstrate of the viral 2A cysteine protease (2A pro ) and inhibited its activity. This peptide was chemically modified with a reactive electrophilic fluoromethylketone group to form a covalent linkage with the nucleophilic active-site thiol of the enzyme. Ex vivo and in vivo experiments showed that thus converted, LVLQTM was a strong inhibitor of HRV replication in both A549 cells and mice. To our knowledge, this is the first report validating a compound against HRV infection in a mouse model.

Published
2012
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8. Physiological relevance and contribution to metal balance of specific and non-specific Metallothionein isoforms in the garden snail, Cantareus aspersus

Author

Reinhard Dallinger, Sílvia Pérez-Rafael, Annette de Vaufleury, Martina Höckner, Karin Stefanon, Òscar Palacios, Sílvia Atrian, Freddy Monteiro, Mercè Capdevila, Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), Institut für Zoologie, Universität Innsbruck [Innsbruck], Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), and Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)

Subjects
MESH : Molecular Sequence Data, Transcription, Genetic, [ SDV.TOX.ECO ] Life Sciences [q-bio]/Toxicology/Ecotoxicology, MESH: Amino Acid Sequence, MESH: Protein Isoforms, 010501 environmental sciences, 01 natural sciences, Mass Spectrometry, MESH: Recombinant Proteins, Transcription (biology), MESH: Helix (Snails), Metallothionein, Protein Isoforms, MESH: Animals, MESH : Copper, Peptide sequence, Chromatography, High Pressure Liquid, MESH : Cadmium, 0303 health sciences, Cadmium, biology, Ecology, MESH : Amino Acid Sequence, MESH : Sequence Alignment, Metals and Alloys, Recombinant Proteins, MESH: Copper, Biochemistry, MESH : Helix (Snails), [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology, General Agricultural and Biological Sciences, Gene isoform, MESH : Recombinant Proteins, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Cadmium, chemistry.chemical_element, Sequence alignment, Pulmonata, General Biochemistry, Genetics and Molecular Biology, Biomaterials, 03 medical and health sciences, MESH : Chromatography, High Pressure Liquid, MESH : Mass Spectrometry, Animals, Amino Acid Sequence, MESH: Chromatography, High Pressure Liquid, Gene, 030304 developmental biology, 0105 earth and related environmental sciences, MESH: Mass Spectrometry, MESH: Molecular Sequence Data, MESH: Transcription, Genetic, Helix, Snails, MESH: Metallothionein, MESH : Transcription, Genetic, MESH : Protein Isoforms, biology.organism_classification, MESH : Metallothionein, chemistry, MESH : Animals, Sequence Alignment, Copper
Abstract

International audience; Variable environmental availability of metal ions represents a constant challenge for most organisms, so that during evolution, they have optimised physiological and molecular mechanisms to cope with this particular requirement. Metallothioneins (MTs) are proteins that play a major role in metal homeostasis and as a reservoir. The MT gene/protein systems of terrestrial helicid snails are an invaluable model for the study of metal-binding features and MT isoform-specific functionality of these proteins. In the present study, we characterised three paralogous MT isogenes and their expressed products in the escargot (Cantareus aspersus). The metal-dependent transcriptional activation of the three isogenes was assessed using quantitative Real Time PCR. The metal-binding capacities of the three isoforms were studied by characterising the purified native complexes. All the data were analysed in relation to the trace element status of the animals after metal feeding. Two of the three C. aspersus MT (CaMT) isoforms appeared to be metal-specific, (CaCdMT and CaCuMT, for cadmium and copper respectively). A third isoform (CaCd/CuMT) was non-specific, since it was natively recovered as a mixed Cd/Cu complex. A specific role in Cd detoxification for CaCdMT was revealed, with a 80-90% contribution to the Cd balance in snails exposed to this metal. Conclusive data were also obtained for the CaCuMT isoform, which is involved in Cu homeostasis, sharing about 30-50% of the Cu balance of C. aspersus. No apparent metal-related physiological function was found for the third isoform (CaCd/CuMT), so its contribution to the metal balance of the escargot may be, if at all, of only marginal significance, but may enclose a major interest in evolutionary studies.

Published
2011
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9. A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane

Author

Kyriakos Kokkoris, Vincent Vincenzetti, Josselin Moosbrugger, Olivier Hachet, Sophie G. Martin, Martine Berthelot-Grosjean, Université de Lausanne, Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Université de Lausanne (UNIL), Centre National de la Recherche Scientifique (CNRS)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB), Centre des Sciences du Goût et de l'Alimentation [Dijon] ( CSGA ), and Institut National de la Recherche Agronomique ( INRA ) -Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH : Molecular Sequence Data, [SDV]Life Sciences [q-bio], Cell, MESH: Cell Cycle, MESH: Amino Acid Sequence, Amino Acid Sequence, Cell Cycle, Cell Membrane/metabolism, Microtubule-Associated Proteins/metabolism, Molecular Sequence Data, Phosphorylation, Protein Kinases/chemistry, Protein Kinases/metabolism, Schizosaccharomyces/cytology, Schizosaccharomyces/metabolism, Schizosaccharomyces pombe Proteins/metabolism, Sequence Alignment, MESH : Phosphorylation, 0302 clinical medicine, 0303 health sciences, Kinase, MESH : Amino Acid Sequence, MESH : Sequence Alignment, Cortical gradient, MESH : Schizosaccharomyces pombe Proteins, Fission yeast, Cell biology, medicine.anatomical_structure, MESH: Schizosaccharomyces, Pom1, Microtubule-Associated Proteins, MESH : Cell Membrane, MESH: Sequence Alignment, MESH : Protein Kinases, Biology, General Biochemistry, Genetics and Molecular Biology, Dephosphorylation, 03 medical and health sciences, Microtubule, MESH : Cell Cycle, Schizosaccharomyces, Cell cortex, medicine, Mitosis, MESH: Protein Kinases, 030304 developmental biology, MESH: Molecular Sequence Data, [ SDV ] Life Sciences [q-bio], Phosphorylation cycle, MESH: Phosphorylation, Biochemistry, Genetics and Molecular Biology(all), Cell Membrane, MESH: Schizosaccharomyces pombe Proteins, MESH: Microtubule-Associated Proteins, MESH : Schizosaccharomyces, MESH : Microtubule-Associated Proteins, Schizosaccharomyces pombe Proteins, DYRK family kinase, Protein Kinases, 030217 neurology & neurosurgery, MESH: Cell Membrane
Abstract

http://linkinghub.elsevier.com/; International audience; Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. Pom1 autophosphorylates in this region to lower lipid affinity and promote membrane release. Tea4 triggers Pom1 plasma membrane association by promoting its dephosphorylation through the protein phosphatase 1 Dis2. We propose that local dephosphorylation induces Pom1 membrane association and nucleates a gradient shaped by the opposing actions of lateral diffusion and autophosphorylation-dependent membrane detachment.

Published
2011
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10. Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions

Author

Palmer Taylor, Pascale Marchot, Géraldine Ferracci, Sandrine Conrod, Philippe Leone, Yves Bourne, Davide Comoletti, Simon U Garcia, Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Université de Provence - Aix-Marseille 1, Department of pharmacology, University of California [San Diego] (UC San Diego), University of California (UC)-University of California (UC), Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), University of California-University of California, Architecture et fonction des macromolécules biologiques ( AFMB ), Centre National de la Recherche Scientifique ( CNRS ) -Aix Marseille Université ( AMU ) -Institut National de la Recherche Agronomique ( INRA ), University of California [San Diego] ( UC San Diego ), Centre de recherche en neurobiologie - neurophysiologie de Marseille ( CRN2M ), and Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
Models, Molecular, MESH : Molecular Sequence Data, Neurexin, MESH : Alternative Splicing, Neuroligin, Plasma protein binding, MESH: Amino Acid Sequence, Crystallography, X-Ray, MESH: Synapses, MESH: Protein Structure, Tertiary, [ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], 0302 clinical medicine, MESH: Nerve Tissue Proteins, Surface plasmon resonance, MESH : Nerve Tissue Proteins, 0303 health sciences, MESH : Amino Acid Sequence, MESH : Sequence Alignment, General Neuroscience, MESH: Alternative Splicing, MESH : Protein Binding, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], MESH: Surface Plasmon Resonance, Dissociation constant, Biochemistry, MESH: Membrane Proteins, MESH : Surface Plasmon Resonance, MESH : Carrier Proteins, MESH : Protein Structure, Tertiary, MESH : Synapses, MESH: Models, Molecular, Protein Binding, MESH : Models, Molecular, Cell Adhesion Molecules, Neuronal, Molecular Sequence Data, MESH: Sequence Alignment, Sequence alignment, Nerve Tissue Proteins, MESH: Carrier Proteins, Biology, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, Humans, MESH: Protein Binding, Amino Acid Sequence, Binding site, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, MESH : Protein Processing, Post-Translational, 030304 developmental biology, Binding Sites, MESH: Humans, MESH: Molecular Sequence Data, General Immunology and Microbiology, MESH : Humans, Alternative splicing, Membrane Proteins, Surface Plasmon Resonance, MESH: Crystallography, X-Ray, Protein Structure, Tertiary, Alternative Splicing, MESH: Binding Sites, MESH : Membrane Proteins, MESH: Protein Processing, Post-Translational, Synapses, Biophysics, MESH : Crystallography, X-Ray, Carrier Proteins, Protein Processing, Post-Translational, Sequence Alignment, MESH : Binding Sites, 030217 neurology & neurosurgery
Abstract

International audience; The extracellular domains of neuroligins and neurexins interact through Ca(2+) to form flexible trans-synaptic associations characterized by selectivity for neuroligin or neurexin subtypes. This heterophilic interaction, essential for synaptic maturation and differentiation, is regulated by gene selection, alternative mRNA splicing and post-translational modifications. A new, 2.6 A-resolution crystal structure of a soluble neurexin-1beta-neuroligin-4 (Nrx1beta-NL4) complex permits a detailed description of the Ca(2+)-coordinated interface and unveils concerted positional rearrangements of several residues of NL4, not observed in neuroligin-1, associated with Nrx1beta binding. Surface plasmon resonance analysis of the binding of structure-guided Nrx1beta mutants towards NL4 and neuroligin-1 shows that flexibility of the Nrx1beta-binding site in NL4 is reflected in a greater dissociation constant of the complex and higher sensitivity to ionic strength and pH variations. Analysis of neuroligin mutants points to critical functions for two respective residues in neuroligin-1 and neuroligin-2 in governing the affinity of the complexes. Although neuroligin-1 and neuroligin-2 have pre-determined conformations that respectively promote and prevent Nrx1beta association, unique conformational reshaping of the NL4 surface is required to permit Nrx1beta association.

Published
2010
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11. Insight into the structure of the pUL89 C-terminal domain of the human cytomegalovirus terminase complex

Author

Couvreux, S, Hantz, S., Marquant, R., Champier, G., Alain, S., Morellet, N., Bouaziz, S., Couvreux, A., Teaching hospital, CHU Limoges, Ecosystèmes forestiers (UR EFNO), Institut national de recherche en sciences et technologies pour l'environnement et l'agriculture (IRSTEA), Institut d'électronique fondamentale (IEF), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Raherison, Sophie, Unité de Pharmacologie Chimique et Génétique (UPCG - UMR_S 640/UMR 8151), Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut de Recherche pour le Développement (IRD)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biologie moléculaire et cellulaire des microorganismes (EA3175), Université de Limoges (UNILIM)-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de Bactériologie, Virologie, Hygiène [CHU Limoges], Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5)-Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC), Centre National de la Recherche Scientifique (CNRS) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Université Paris Descartes - Paris 5 (UPD5) - Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut National de la Santé et de la Recherche Médicale (INSERM) - Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP) - Centre National de la Recherche Scientifique (CNRS) - Institut de Recherche pour le Développement (IRD) - Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP) - Centre National de la Recherche Scientifique (CNRS) - Institut de Recherche pour le Développement (IRD) - Université Paris Descartes - Paris 5 (UPD5), and Université de Limoges (UNILIM) - Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503) - Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, MESH : Molecular Sequence Data, MESH : DNA, Cytomegalovirus, MESH: Protein Structure, Secondary, MESH: Amino Acid Sequence, Protein Structure, Secondary, MESH: Protein Structure, Tertiary, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH: Endonucleases, MESH : RNA, MESH : Endonucleases, MESH : Viral Proteins, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH : Sequence Alignment, MESH : Amino Acid Sequence, MESH: DNA, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH : Protein Structure, Tertiary, MESH: Biocatalysis, MESH: Models, Molecular, MESH: Cytomegalovirus, MESH : Models, Molecular, Molecular Sequence Data, MESH: Sequence Alignment, MESH : Endodeoxyribonucleases, MESH : Cytomegalovirus, Viral Proteins, MESH: RNA, Humans, Amino Acid Sequence, MESH: Endodeoxyribonucleases, Endodeoxyribonucleases, MESH: Humans, MESH: Molecular Sequence Data, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, DNA, Endonucleases, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Viral Proteins, Protein Structure, Tertiary, Biocatalysis, RNA, MESH : Magnetic Resonance Spectroscopy, MESH : Protein Structure, Secondary, MESH : Biocatalysis, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Sequence Alignment
Abstract

International audience; In a previous study, we identified 12 conserved domains within pUL89, the small terminase subunit of the human cytomegalovirus. A latter study showed that the fragment pUL89(580-600) plays an important role in the formation of the terminase complex by interacting with the large terminase subunit pUL56. In this study, analysis was performed to solve the structure of pUL89(568-635) in 50% H2O/50% acetonitrile (v/v). We showed that pUL89(568-635) consists of four alpha helices, but we did not identify any tertiary structure. The fragment 580-600 formed an amphipathic alpha helix, which had a hydrophobic side highly conserved among herpesviral homologs of pUL89; this was not observed for its hydrophilic side. The modeling of pUL89(457-612) using the recognition fold method allowed us to position pUL89(580-600) within this domain. The theoretical structure highlighted three important features. First, we identified a metal-binding pocket containing residues Asp(463), Glu(534), and Glu(588), which are highly conserved among pUL89 homologs. Second, the model predicted a positively charged surface able to interact with the DNA duplex during the nicking event. Third, a hydrophobic patch on the top of the catalytic site suggested that this may constitute part of the pUL89 site recognized by pUL56 potentially involved in DNA binding.

Published
2010
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12. A novel BMP15 variant, potentially affecting the signal peptide, in a familial case of premature ovarian failure

Author

Reiner A. Veitia, Marc Fellous, Rim Braham, Besma Lakhal, Ali Saâd, Hatem Elghezal, Paul Laissue, Service de Cytogénétique, Génétique moléculaire et Biologie de la reproduction, Hôpital Farhat Hached, Institut Cochin (IC UM3 (UMR 8104 / U1016)), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Département d'Endocrinologie, Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut Cochin (UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS), Institut Jacques Monod (IJM), and Université Paris Diderot - Paris 7 (UPD7) - Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH : Molecular Sequence Data, Endocrinology, Diabetes and Metabolism, MESH : Ovarian Failure, Premature, MESH: Amino Acid Sequence, 0302 clinical medicine, Endocrinology, MESH : Female, Peptide sequence, ComputingMilieux_MISCELLANEOUS, [SDV.MHEP.EM] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, 0303 health sciences, 030219 obstetrics & reproductive medicine, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH: Bone Morphogenetic Protein 15, MESH: Genetic Predisposition to Disease, MESH : Adult, [SDV.MHEP.EM]Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, 3. Good health, Premature ovarian failure, MESH: Young Adult, Mutation (genetic algorithm), MESH : Mutation, MESH: Tunisia, MESH: Protein Sorting Signals, Signal peptide, medicine.medical_specialty, MESH: Mutation, MESH: Ovarian Failure, Premature, MESH : Young Adult, MESH: Sequence Alignment, Sequence alignment, Biology, 03 medical and health sciences, Familial case, MESH : Tunisia, Internal medicine, medicine, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Bone morphogenetic protein 15, MESH : Humans, MESH: Adult, medicine.disease, Protein Sorting Signals, MESH : Protein Sorting Signals, MESH : Genetic Predisposition to Disease, MESH : Bone Morphogenetic Protein 15, MESH: Female
Abstract

International audience

Published
2009
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13. HIV-1 gp41-specific monoclonal mucosal IgAs derived from highly exposed but IgG-seronegative individuals block HIV-1 epithelial transcytosis and neutralize CD4(+) cell infection: an IgA gene and functional analysis

Author

L. Diomede, Tudor D, C Moog, Reynes Jm, Anne Sophie Drillet, Houimel M, Lucia Lopalco, Morgane Bomsel, Derrien M, Institut Cochin (UMR_S567 / UMR 8104), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Division of Immunology, Transplantation and Infectious Diseases, San Raffaele Scientific Institute, Pathogénie des infections Virales Persistantes, Université Louis Pasteur - Strasbourg I-Faculté de Médecine-Institut de Virologie, Institut Pasteur du Cambodge, Réseau International des Instituts Pasteur (RIIP), Institut Cochin ( UMR_S567 / UMR 8104 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Pasteur du Cambodge-Réseau International des Instituts Pasteur ( RIIP ), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)

Subjects
Immunoglobulin A, Sexually transmitted disease, CD4-Positive T-Lymphocytes, MESH : Molecular Sequence Data, MESH: HIV Envelope Protein gp41, MESH: Virus Internalization, Sequence Homology, MESH : Vagina, HIV Infections, Cervix Uteri, MESH : Sexual Partners, MESH: Amino Acid Sequence, HIV Antibodies, MESH: Antibodies, Monoclonal, MESH: HIV-1, [ SDV.MP ] Life Sciences [q-bio]/Microbiology and Parasitology, Immunology and Allergy, MESH: Sexual Partners, MESH : Female, MESH : Mucous Membrane, MESH: Sequence Homology, Gene Rearrangement, B-Lymphocyte, MESH: Peptide Fragments, MESH : HIV Seronegativity, Conserved Sequence, MESH: HIV Seronegativity, MESH: Conserved Sequence, biology, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH: Gene Rearrangement, B-Lymphocyte, MESH : Immunoglobulin A, Secretory, Antibodies, Monoclonal, MESH: CD4-Positive T-Lymphocytes, Environmental exposure, MESH: HIV Infections, MESH: Cervix Uteri, MESH : Adult, MESH : Immunity, Innate, HIV Envelope Protein gp41, MESH: Immunoglobulin Fab Fragments, Sexual Partners, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Transcytosis, MESH : Antibodies, Monoclonal, MESH : CD4-Positive T-Lymphocytes, Monoclonal, Vagina, Female, MESH: Immunity, Innate, Antibody, MESH : HIV-1, Adult, Immunology, Molecular Sequence Data, MESH: Environmental Exposure, MESH: Sequence Alignment, Gp41, Immunoglobulin Fab Fragments, MESH : HIV Antibodies, MESH : Immunoglobulin Fab Fragments, Peptide Library, MESH : Peptide Library, MESH : Sequence Homology, MESH : Conserved Sequence, HIV Seronegativity, MESH : HIV Infections, MESH : Virus Internalization, Humans, Amino Acid Sequence, Mucous Membrane, MESH: Molecular Sequence Data, MESH: Humans, MESH: HIV Antibodies, MESH : Humans, MESH : Peptide Fragments, MESH: Mucous Membrane, MESH: Adult, Gene rearrangement, Environmental Exposure, Virus Internalization, Virology, Immunity, Innate, Peptide Fragments, MESH : HIV Envelope Protein gp41, MESH: Immunoglobulin A, Secretory, MESH : Gene Rearrangement, B-Lymphocyte, MESH: Vagina, MESH : Cervix Uteri, Immunoglobulin A, Secretory, biology.protein, HIV-1, MESH: Peptide Library, Sequence Alignment, MESH : Environmental Exposure, MESH: Female
Abstract

International audience; AIDS is mainly a sexually transmitted disease, and accordingly, mucosal tissues are the primary sites of natural human immunodeficiency virus type-1 (HIV-1) transmission. Mucosal immunoglobulin A (IgA) antibody specific for HIV-1 envelope gp41 subunit is one correlate of protection in individuals who are highly sexually exposed to HIV-1 but remain persistently IgG seronegative (HEPS). Understanding these peculiar IgAs at the gene and functional level is possible only with monoclonal IgAs. We have constructed a mucosal Fab IgA library from HEPS and have characterized a series of HIV-1 IgAs specific for gp41 that, in vitro, are transcytosis-blocking and infection-neutralizing. Characterization of their IgA genes shows that Fab specific for the gp41 membrane-proximal region harbors a long heavy-chain CDR3 loop (CDRH3) similar to the two broadly neutralizing IgG monoclonal antibodies, 2F5 and 4E10. Furthermore, the selected Fab IgA shows extensive somatic mutations that cluster in the CDR regions, indicating that affinity maturation due to an antigen-driven process had occurred in HEPS individuals, presumably upon multiple exposures to HIV. This analysis of HEPS monoclonal IgA gives a unique opportunity to correlate an antibody function (resistance to a pathogen in vivo) with an antibody gene. Such neutralizing monoclonal IgAs could be used in microbicide formulation.

Published
2009
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14. Phenotypic spectrum of STRA6 mutations: from Matthew-Wood syndrome to non-lethal anophthalmia

Author

Nicolas, Chassaing, Christelle, Golzio, Sylvie, Odent, Léopoldine, Lequeux, Adeline, Vigouroux, Jelena, Martinovic-Bouriel, Francesco Danilo, Tiziano, Lucia, Masini, Francesca, Piro, Giovanna, Maragliano, Anne-Lise, Delezoide, Tania, Attié-Bitach, Sylvie, Manouvrier-Hanu, Heather C, Etchevers, Patrick, Calvas, Service de génétique médicale, CHU Toulouse [Toulouse]-Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse], Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), IFR Necker-Enfants Malades (IRNEM), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement (Inserm U781), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de génétique clinique, hôpital Sud, Institut de Génétique et Développement de Rennes (IGDR), Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Service de Génétique Médicale [CHU Necker], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Necker - Enfants Malades [AP-HP], Institute of Medical Genetics, Università cattolica del Sacro Cuore [Milano] (Unicatt), Institute of Obstetrics and Gynecology, Operative Unit of Pathology, San Giovanni Ospedale, Complex Unit of Neonatology, Service de Biologie du Développement, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Robert Debré, Laboratoire de Génétique Clinique, Hôpital Jeanne de Flandre [Lille]-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), De Villemeur, Hervé, Service Génétique Médicale [CHU Toulouse], Institut Fédératif de Biologie (IFB), Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Pôle Biologie [CHU Toulouse], Centre Hospitalier Universitaire de Toulouse (CHU Toulouse), Service de génétique clinique [Rennes], Université de Rennes (UR)-CHU Pontchaillou [Rennes]-hôpital Sud, Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Physiopathologie Toulouse Purpan (ex IFR 30 et IFR 150), Université Toulouse III - Paul Sabatier ( UPS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR30-IFR150-Institut National de la Santé et de la Recherche Médicale ( INSERM ), IFR Necker-Enfants Malades ( IRNEM ), Assistance publique - Hôpitaux de Paris (AP-HP)-Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement ( Inserm U781 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Hôpital Sud, Institut de Génétique et Développement de Rennes ( IGDR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -IFR140-Centre National de la Recherche Scientifique ( CNRS ), Assistance publique - Hôpitaux de Paris (AP-HP)-CHU Necker - Enfants Malades [AP-HP], Università Cattolica del Sacro Cuore, Assistance publique - Hôpitaux de Paris (AP-HP)-Hôpital Robert Debré, and Hôpital Jeanne de Flandre [Lille]-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] ( CHRU Lille )

Subjects
Male, MESH: Fatal Outcome, MESH : Molecular Sequence Data, MESH: Anophthalmos, [SDV.GEN] Life Sciences [q-bio]/Genetics, MESH: Amino Acid Sequence, Settore MED/03 - GENETICA MEDICA, MESH : Syndrome, Fatal Outcome, MESH : Female, MESH: Syndrome, [SDV.BDD]Life Sciences [q-bio]/Development Biology, MESH : Sequence Alignment, MESH : Amino Acid Sequence, MESH : Infant, Syndrome, MESH : Adult, MESH: Infant, MESH : Phenotype, Phenotype, Female, MESH: Membrane Proteins, MESH : Mutation, Adult, MESH: Abnormalities, Multiple, MESH: Mutation, stra6, MESH : Male, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Phenotype, [SDV.BDD] Life Sciences [q-bio]/Development Biology, Humans, Abnormalities, Multiple, Amino Acid Sequence, [ SDV.BDD ] Life Sciences [q-bio]/Development Biology, [SDV.GEN]Life Sciences [q-bio]/Genetics, MESH: Molecular Sequence Data, MESH: Humans, MESH : Abnormalities, Multiple, MESH : Humans, MESH : Anophthalmos, Anophthalmos, Infant, Membrane Proteins, MESH: Adult, MESH: Male, MESH : Fatal Outcome, MESH : Membrane Proteins, Mutation, [ SDV.GEN ] Life Sciences [q-bio]/Genetics, Sequence Alignment, MESH: Female
Abstract

International audience; Matthew-Wood, Spear, PDAC or MCOPS9 syndrome are alternative names used to refer to combinations of microphthalmia/anophthalmia, malformative cardiac defects, pulmonary dysgenesis, and diaphragmatic hernia. Recently, mutations in STRA6, encoding a membrane receptor for vitamin A-bearing plasma retinol binding protein, have been identified in such patients. We performed STRA6 molecular analysis in three fetuses and one child diagnosed with Matthew-Wood syndrome and in three siblings where two adult living brothers are affected with combinations of clinical anophthalmia, tetralogy of Fallot, and mental retardation. Among these patients, six novel mutations were identified, bringing the current total of known STRA6 mutations to seventeen. We extensively reviewed clinical data pertaining to all twenty-one reported patients with STRA6 mutations (the seven of this report and fourteen described elsewhere) and discuss additional features that may be part of the syndrome. The clinical spectrum associated with STRA6 deficiency is even more variable than initially described.

Published
2009
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15. Epidemiological surveillance of mycoplasmas belonging to the 'Mycoplasma mycoides' cluster: is DGGE fingerprinting of 16S rRNA genes suitable?

Author

Laure Maigre, François Poumarat, A. Tricot, Florence Tardy, Patrice Gaurivaud, Laboratoire d'études et de recherches en pathologie bovine et hygiène des viandes, AFSSA, Mycoplasmoses des ruminants [Lyon], Université de Lyon-VetAgro Sup ( VAS ), Agence Française de Sécurité Sanitaire des Aliments (AFSSA), Mycoplasmoses des Ruminants - UMR (MYCO), and Université de Lyon-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)

Subjects
MESH : Mycoplasma Infections, MESH : Molecular Sequence Data, 16SrRNA gene, MESH: Base Sequence, [ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, medicine.disease_cause, Applied Microbiology and Biotechnology, strains detection and identification, MESH: Mycoplasma, Mycoplasma, MESH : Cattle, RNA, Ribosomal, 16S, MESH: Cattle Diseases, MESH: DNA Fingerprinting, MESH : DNA, Ribosomal, MESH : DNA, Bacterial, MESH: Animals, 1UMYCOPLASME, DGGE, MESH: Phylogeny, Phylogeny, MESH: DNA, Ribosomal, biology, Phylogenetic tree, MESH : Sequence Alignment, Goats, epidemiological surveillance, [ SDV.SPEE ] Life Sciences [q-bio]/Santé publique et épidémiologie, MESH : DNA Fingerprinting, MESH: RNA, Ribosomal, 16S, MESH: Cattle, "Mycoplasma mycoides" cluster, Electrophoresis, Polyacrylamide Gel, Mycoplasma mycoides, Temperature gradient gel electrophoresis, DNA, Bacterial, Sequence analysis, Molecular Sequence Data, MESH: Sequence Alignment, Cattle Diseases, MESH : Goat Diseases, MESH: Goat Diseases, MESH : Electrophoresis, Polyacrylamide Gel, MESH: Goats, DNA, Ribosomal, MYCOPLASME, Microbiology, Phylogenetics, medicine, Animals, Humans, Mycoplasma Infections, MESH : Cattle Diseases, MESH: Humans, MESH: Molecular Sequence Data, MESH : Mycoplasma, Goat Diseases, Base Sequence, MESH : Humans, MESH : Phylogeny, Ribosomal RNA, MESH: Mycoplasma Infections, biology.organism_classification, 16S ribosomal RNA, MESH: DNA, Bacterial, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, DNA Fingerprinting, MESH : RNA, Ribosomal, 16S, MESH : Goats, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, Mycoplasma mycoides" cluster, MESH : Base Sequence, Cattle, MESH : Animals, Sequence Alignment, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

Aims: The analysis by Denaturing Gradient Gel Electrophoresis (DGGE) of the PCR-amplified V3 region of 16S rRNA gene was previously shown to detect and differentiate a large number of human and animal mycoplasmas. In this study, we further assessed the suitability of the technique for epidemiological surveillance of mycoplasmas belonging to the ‘Mycoplasma mycoides’ cluster, a phylogenetic group that includes major ruminant pathogens. Methods and Results: The V3 region of 16S rRNA genes from approx. 50 field strains was amplified and analysed by DGGE. Detection and identification results were compared with the ones obtained by antigenic testing and sequence analysis. Conclusions: The DGGE technique is robust and valuable as a first-line test, but the patterns obtained for strains belonging to the ‘M. mycoides’ cluster were too variable within a taxon and in contrast too conserved between taxa to allow an unequivocal identification of isolates without further analysis. Significance and Impact of the Study: Issues raised by the quest for a single universal test able to detect and identify any mycoplasma in one clinical sample are thoroughly documented.

Published
2008
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16. Aichi virus, norovirus, astrovirus, enterovirus, and rotavirus involved in clinical cases from a French oyster-related gastroenteritis outbreak

Author

Katia Ambert-Balay, Robert L. Atmar, Ophelie Serais, Monique Pommepuy, Sylvain Parnaudeau, H. Giraudon, Joanna Krol, G Delmas, Jean-Claude Le Saux, Françoise S. Le Guyader, Pierre Pothier, Laboratoire de Microbiologie, IFREMER, Institut Français de Recherche pour l'Exploitation de la Mer ( IFREMER ), Laboratoire Interactions Muqueuses Agents Transmissibles ( LIMA ), Université de Bourgogne ( UB ), Laboratoire de sérologie-virologie (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER), Laboratoire Interactions Muqueuses Agents Transmissibles (LIMA), Université de Bourgogne (UB), and Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)

Subjects
Male, Rotavirus, Oyster, MESH : Molecular Sequence Data, Epidemiology, viruses, MESH: Base Sequence, medicine.disease_cause, MESH : Kobuvirus, Disease Outbreaks, Feces, MESH: Animals, MESH : Female, MESH: Disease Outbreaks, Enterovirus, 0303 health sciences, MESH: Middle Aged, biology, MESH: Kobuvirus, MESH : Sequence Alignment, MESH: Enterovirus, MESH: Feces, food and beverages, MESH: Rotavirus, Middle Aged, MESH : Adult, Gastroenteritis, 3. Good health, MESH : Gastroenteritis, MESH: Virus Diseases, Virus Diseases, MESH: RNA, Viral, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, RNA, Viral, Female, MESH : Enterovirus, France, Aichi virus, Adult, Microbiology (medical), MESH: Norovirus, Kobuvirus, MESH : Male, MESH : Rotavirus, Molecular Sequence Data, MESH: Sequence Alignment, Reoviridae, [ SDV.MP.VIR ] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Ostreidae, Microbiology, Astrovirus, 03 medical and health sciences, biology.animal, medicine, Animals, Humans, MESH : RNA, Viral, MESH : Middle Aged, MESH : Disease Outbreaks, MESH : France, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Humans, MESH : Ostreidae, Base Sequence, 030306 microbiology, MESH : Norovirus, Norovirus, MESH : Humans, MESH: Adult, MESH : Feces, biology.organism_classification, MESH : Virus Diseases, Ostreidae, Virology, Caliciviridae, MESH: Male, MESH: Gastroenteritis, MESH: France, MESH : Base Sequence, MESH : Animals, Sequence Alignment, MESH: Female
Abstract

Following a flooding event close to a shellfish production lagoon, 205 cases of gastroenteritis were linked to oyster consumption. Twelve stool samples from different individuals were collected. Analysis showed that eight samples were positive for multiple enteric viruses, and one stool sample had seven different enteric viruses. Analysis of shellfish implicated in the outbreak allowed detection of the same diversity of enteric viruses, with some viral genomic sequences being identical to those obtained from stool sample analysis. Shellfish were contaminated by as many as five different enteric viruses. For the first time in Europe, Aichi virus was identified in oyster samples. Shellfish samples collected over 3 weeks following the outbreak showed a progressive decline in the level of virus contamination as measured by the virus diversity detected and by quantitative reverse transcription-PCR.

Published
2008
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17. Ancient DNA evidence for the loss of a highly divergent brown bear clade during historical times

Author

Calvignac, Sébastien, Hughes, Sandrine, Tougard, Christelle, Michaux, Jacques, Thevenot, Michel, Philippe, Michel, Hamdine, Watik, Hänni, Catherine, Institut de Génomique Fonctionnelle de Lyon (IGFL), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Biogéosciences [UMR 6282] [Dijon] (BGS), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Centre d’Ecologie Fonctionnelle et Evolutive (CEFE), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Université Paul-Valéry - Montpellier 3 (UPVM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut de Recherche pour le Développement (IRD [France-Sud]), Centre de Conservation et d'Étude sur les Collections (CCEC), Muséeum d'Histoire Naturelle, Work supported by the CNRS (eclipse program), University Lyon I and the programme ‘Dynamique évolutive des espèces fractionnées, insulaires et invasives' of the EPHE. Contribution ISEM 2006–085., Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Université Paul-Valéry - Montpellier 3 (UM3)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Biogéosciences [UMR 6282] (BGS), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École Pratique des Hautes Études (EPHE), Université Paul-Valéry - Montpellier 3 (UPVM)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut de Génomique Fonctionnelle de Lyon ( IGFL ), École normale supérieure - Lyon ( ENS Lyon ) -Institut National de la Recherche Agronomique ( INRA ) -Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Biogéosciences [Dijon] ( BGS ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Institut des Sciences de l'Evolution de Montpellier ( ISEM ), Université de Montpellier ( UM ) -Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique ( CNRS ), Centre d’Ecologie Fonctionnelle et Evolutive ( CEFE ), Université Paul-Valéry - Montpellier 3 ( UM3 ) -Centre international d'études supérieures en sciences agronomiques ( Montpellier SupAgro ) -École pratique des hautes études ( EPHE ) -Institut national de la recherche agronomique [Montpellier] ( INRA Montpellier ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD [France-Sud] ) -Institut national d’études supérieures agronomiques de Montpellier ( Montpellier SupAgro ), and Centre de Conservation et d'Étude sur les Collections ( CCEC )

Subjects
MESH : Molecular Sequence Data, MESH : Cytochromes b, MESH: Africa, Northern, brown bear, phylogeography, MESH: Base Sequence, [SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy, Polymerase Chain Reaction, MESH: Fossils, MESH: Variation (Genetics), MESH: Extinction, Biological, Africa, Northern, MESH : DNA, Mitochondrial, MESH: Animals, MESH: Phylogeny, MESH : Ursidae, MESH : Polymerase Chain Reaction, Phylogeny, [ SDU.STU.PG ] Sciences of the Universe [physics]/Earth Sciences/Paleontology, MESH : Variation (Genetics), Fossils, mtDNA, MESH : Sequence Alignment, Cytochromes b, MESH: Cytochromes b, MESH : Africa, Northern, [ SDV.GEN.GPO ] Life Sciences [q-bio]/Genetics/Populations and Evolution [q-bio.PE], MESH : Extinction, Biological, [SDU.STU.PG]Sciences of the Universe [physics]/Earth Sciences/Paleontology, Ursidae, MESH: Ursidae, Molecular Sequence Data, MESH: Sequence Alignment, Extinction, Biological, DNA, Mitochondrial, Animals, ancient DNA, MESH: Molecular Sequence Data, [SDV.GEN.GPO]Life Sciences [q-bio]/Genetics/Populations and Evolution [q-bio.PE], Base Sequence, Holocene, MESH: DNA, Mitochondrial, MESH : Phylogeny, Genetic Variation, MESH: Polymerase Chain Reaction, North Africa, MESH : Fossils, MESH : Base Sequence, MESH : Animals, Sequence Alignment, human activities, [ SDV.BID.SPT ] Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy
Abstract

9 pages; International audience; The genetic diversity of present-day brown bears (Ursus arctos) has been extensively studied over the years and appears to be geographically structured into five main clades. The question of the past diversity of the species has been recently addressed by ancient DNA studies that concluded to a relative genetic stability over the last 35,000 years. However, the post-last glacial maximum genetic diversity of the species still remains poorly documented, notably in the Old World. Here, we analyse Atlas brown bears, which became extinct during the Holocene period. A divergent brown bear mitochondrial DNA lineage not present in any of the previously studied modern or ancient bear samples was uncovered, suggesting that the diversity of U. arctos was larger in the past than it is now. Specifically, a significant portion (with respect to sequence divergence) of the intraspecific diversity of the brown bear was lost with the extinction of the Atlas brown bear after the Pleistocene/Holocene transition.

Published
2008
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18. Cloning and expression of genes involved in conidiation and surface properties of Penicillium camemberti grown in liquid and solid cultures

Author

Jean-François Cavin, Dominique Garmyn, Khadidja Boualem, Yves Waché, Patrick Gervais, A. Durand, Thomas Karbowiak, Génie des Procédés Microbiologiques et Alimentaires ( GPMA ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Laboratoire de Microbioologie, UMR INRA 1283 Ecole Nationale Supérieure de Biologie Appliquée à la. Nutrition et à l'Alimentation, Institut National de la Recherche Agronomique ( INRA ), Laboratoire de Microbiologie, UMR INRA 1082, AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Génie des Procédés Microbiologiques et Alimentaires (GPMA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Laboratoire de Microbioologie, and Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)

Subjects
MESH: Sequence Analysis, DNA, MESH : Spores, Fungal, MESH : Molecular Sequence Data, Conidiation, MESH: Amino Acid Sequence, MESH: Base Sequence, Gene Expression Regulation, Fungal, Gene expression, MESH : Fungal Proteins, Cloning, Molecular, Fungal protein, MESH : Amino Acid Sequence, MESH : Sequence Alignment, General Medicine, Spores, Fungal, MESH: Mycelium, Cell biology, Weta, Penicillium camemberti, MESH: Fungal Proteins, MESH : Hydrophobicity, Hydrophobic and Hydrophilic Interactions, MESH : Mycelium, MESH: Gene Expression Regulation, Fungal, Hypha, MESH : Cloning, Molecular, Hydrophobin, Molecular Sequence Data, MESH: Sequence Alignment, Biology, Microbiology, Fungal Proteins, MESH: Spores, Fungal, MESH : Gene Expression Regulation, Fungal, MESH: Cloning, Molecular, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Molecular Biology, Gene, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Penicillium, MESH: Hydrophobicity, MESH: Molecular Sequence Data, Base Sequence, Mycelium, Penicillium, Sequence Analysis, DNA, MESH : Penicillium, biology.organism_classification, Culture Media, MESH: Culture Media, MESH : Base Sequence, MESH : Culture Media, Sequence Alignment, MESH : Sequence Analysis, DNA
Abstract

International audience; Based on bioinformatic data on model fungi, the rodA and wetA genes encoding, respectively, a RodA hydrophobin protein and the WetA protein involved in conidiation mechanisms, were PCR-cloned and characterized for the first time in Penicillium camemberti. These results, completed by a sequence of the brlA gene (available in GenBank), which encodes a major transcriptional regulator also involved in the conidiation mechanism, were used to compare, by qRT-PCR, the expression of the three genes in liquid and solid cultures in a synthetic medium. While expression of the brlA and wetA genes increased dramatically in both culture conditions after 4 days of growth, expression of the rodA gene increased only with conidiation and in the solid culture, and this expression was correlated with production and secretion of a RodA protein outside the hyphae, which became very hydrophobic. In liquid cultures, no production of RodA occurred in mycelia, which remained hydrophilic, and no conidiation was detected despite formation of swellings at the tips of hyphae. The absence of conidiation in liquid culture correlated with the lack of rodA gene expression, which could be regulated by the medium composition independently of brlA and wetA genes expression.

Published
2008
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19. Molecular and biochemical characterization of a cathepsin B-like protease family unique to Trypanosoma congolense

Author

Edith Authié, Théo Baltz, Theresa H.T. Coetzer, Nicolas Biteau, Virginie Coustou, C. Giroud, Carlos Mendoza-Palomares, Alain Boulangé, Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Microbiologie cellulaire et moléculaire et pathogénicité (MCMP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Laboratoire biologie moléculaire et immunologie de protozoaires parasites, Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5) - Centre National de la Recherche Scientifique (CNRS), Université Bordeaux Segalen - Bordeaux 2 - Centre National de la Recherche Scientifique (CNRS), Université de Lyon - Université de Lyon - Centre National de la Recherche Scientifique (CNRS), ProdInra, Migration, Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS), Programme forêts naturelles (Cirad-Forêt programme Forêts naturelles), Département Forêt (Cirad-FORET), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Infectiologie Animale et Santé Publique (UR IASP), Institut National de la Recherche Agronomique (INRA), UMR Trypanosomes, Institut de Recherche pour le Développement (IRD)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Département Systèmes Biologiques (Cirad-BIOS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), and Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)

Subjects
MESH : Molecular Sequence Data, Trypanosoma congolense, [SDV]Life Sciences [q-bio], Cathepsin E, MESH: Amino Acid Sequence, Cathepsin F, L73 - Maladies des animaux, Cathepsin A, Cathepsin B, Cathepsin C, MESH: Recombinant Proteins, 0302 clinical medicine, Cathepsin O, Cathepsin H, Cathepsin L1, Immunologie, MESH: Animals, MESH: Phylogeny, Phylogeny, 0303 health sciences, MESH : Amino Acid Sequence, MESH : Sequence Alignment, Contrôle de maladies, MESH : Trypanosoma congolense, Cystéine, General Medicine, Articles, MESH: Trypanosoma congolense, Recombinant Proteins, 3. Good health, [SDV] Life Sciences [q-bio], [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, PCR, Biochemistry, Multigene Family, Protéase, MESH : Recombinant Proteins, 030231 tropical medicine, Molecular Sequence Data, MESH : Multigene Family, MESH: Sequence Alignment, MESH : Cathepsins, Biology, Microbiology, 03 medical and health sciences, Animals, Peptidase, Amino Acid Sequence, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, Molecular Biology, 030304 developmental biology, MESH: Molecular Sequence Data, Anticorps, MESH : Phylogeny, Molecular biology, Cathepsins, MESH: Cathepsins, MESH: Multigene Family, MESH : Animals, Sequence Alignment
Abstract

Cysteine proteases have been shown to be essential virulence factors and drug targets in trypanosomatids and an attractive antidisease vaccine candidate forTrypanosoma congolense. Here, we describe an important amplification of genes encoding cathepsin B-like proteases unique toT. congolense. More than 13 different genes were identified, whereas only one or two highly homologous genes have been identified in other trypanosomatids. These proteases grouped into three evolutionary clusters: TcoCBc1 to TcoCBc5 and TcoCBc6, which possess the classical catalytic triad (Cys, His, and Asn), and TcoCBs7 to TcoCBs13, which contains an unusual catalytic site (Ser, Xaa, and Asn). Expression profiles showed that members of the TcoCBc1 to TcoCBc5 and the TcoCBs7 to TcoCBs13 groups are expressed mainly in bloodstream forms and localize in the lysosomal compartment. The expression of recombinant representatives of each group (TcoCB1, TcoCB6, and TcoCB12) as proenzymes showed that TcoCBc1 and TcoCBc6 are able to autocatalyze their maturation 21 and 31 residues, respectively, upstream of the predicted start of the catalytic domain. Both displayed a carboxydipeptidase function, while only TcoCBc1 behaved as an endopeptidase. TcoCBc1 exhibited biochemical differences regarding inhibitor sensitivity compared to that of other cathepsin B-like proteases. Recombinant pro-TcoCBs12 did not automature in vitro, and the pepsin-matured enzyme was inactive in tests with cathepsin B fluorogenic substrates. In vivo inhibition studies using CA074Me (a cell-permeable cathepsin B-specific inhibitor) demonstrated that TcoCB are involved in lysosomal protein degradation essential for survival in bloodstream form. Furthermore, TcoCBc1 elicited an important immune response in experimentally infected cattle. We propose this family of proteins as a potential therapeutic target and as a plausible antigen forT. congolensediagnosis.

Published
2008
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20. A RasGAP SH3 peptide aptamer inhibits RASGAP-Aurora interaction and induces caspase-independent tumor cell death

Author

Pierre Colas, Anne-Laure Mathieu, Françoise Raynaud, Perayot Pamonsinlapatham, Olivier Moncorgé, Réda Hadj-Slimane, Perrine Mercier, Yves Lepelletier, Audrey Barthelaix, Claudine Corneloup, Ivan Mikaelian, Jerome Samson, Marc Bickle, Christiane Garbay, Sylvie Dufour, Matthieu Schapira, Nicolas Hugo, Cytokines, hématopoïèse et réponse immune (CHRI), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Pharmacochimie Moléculaire et Cellulaire (PMC - UMR_S 648), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5), Aptanomics, Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Favey, Allison, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS), Pharmacochimie Moléculaire et Cellulaire ( PMC - UMR_S 648 ), Centre National de la Recherche Scientifique ( CNRS ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Paris Descartes - Paris 5 ( UPD5 ), Cytokines, hématopoïèse et réponse immune ( CHRI ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Compartimentation et dynamique cellulaires ( CDC ), Centre National de la Recherche Scientifique ( CNRS ) -INSTITUT CURIE-Université Pierre et Marie Curie - Paris 6 ( UPMC ), and Slama, Catherine

Subjects
MESH : Molecular Sequence Data, MESH : ras GTPase-Activating Proteins, Cell Biology/Cell Growth and Division, lcsh:Medicine, Peptide, MESH: Amino Acid Sequence, Biochemistry, MESH: ras GTPase-Activating Proteins, 0302 clinical medicine, Aurora Kinases, lcsh:Science, MESH: Peptide Fragments, Peptide sequence, Conserved Sequence, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, 0303 health sciences, Multidisciplinary, MESH: Conserved Sequence, Effector, MESH : Amino Acid Sequence, MESH : Sequence Alignment, Cell Biology/Cellular Death and Stress Responses, ras GTPase-Activating Proteins, Caspases, 030220 oncology & carcinogenesis, Biochemistry/Drug Discovery, Research Article, Proto-oncogene tyrosine-protein kinase Src, MESH : Protein-Serine-Threonine Kinases, MESH : Recombinant Fusion Proteins, Recombinant Fusion Proteins, Aptamer, Molecular Sequence Data, Aurora B kinase, MESH: Sequence Alignment, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Protein Serine-Threonine Kinases, Biology, MESH: Protein-Serine-Threonine Kinases, Protein–protein interaction, 03 medical and health sciences, MESH : Conserved Sequence, MESH: Recombinant Fusion Proteins, Amino Acid Sequence, Binding site, Molecular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, 030304 developmental biology, Binding Sites, MESH: Caspases, MESH: Molecular Sequence Data, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH : Peptide Fragments, lcsh:R, Biochemistry/Chemical Biology of the Cell, Peptide Fragments, chemistry, MESH: Binding Sites, lcsh:Q, MESH : Caspases, Sequence Alignment, MESH : Binding Sites
Abstract

International audience; The Ras GTPase-activating protein RasGAP catalyzes the conversion of active GTP-bound Ras into inactive GDP-bound Ras. However, RasGAP also acts as a positive effector of Ras and exerts an anti-apoptotic activity that is independent of its GAP function and that involves its SH3 (Src homology) domain. We used a combinatorial peptide aptamer approach to select a collection of RasGAP SH3 specific ligands. We mapped the peptide aptamer binding sites by performing yeast two-hybrid mating assays against a panel of RasGAP SH3 mutants. We examined the biological activity of a peptide aptamer targeting a pocket delineated by residues D295/7, L313 and W317. This aptamer shows a caspase-independent cytotoxic activity on tumor cell lines. It disrupts the interaction between RasGAP and Aurora B kinase. This work identifies the above-mentioned pocket as an interesting therapeutic target to pursue and points its cognate peptide aptamer as a promising guide to discover RasGAP small-molecule drug candidates.

Published
2008
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21. Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis

Author

Mustapha Cherkaoui-Malki, Pierre Andreoletti, Driss Mountassif, Adnane Moutaouakkil, Zakaria El Kebbaj, M'Hammed Saïd El Kebbaj, Norbert Latruffe, Laboratoire Biochimie et Biologie Moléculaire ( LBBM ), Université Hassan II, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Latruffe, Norbert, Laboratoire Biochimie et Biologie Moléculaire (LBBM), Université Hassan II [Casablanca] (UH2MC), Lipides - Nutrition - Cancer (U866) (LNC), and Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)

Subjects
lcsh:Animal biochemistry, MESH : Aged, MESH : Rodentia, MESH: Rodentia, MESH: Base Sequence, Biochemistry, MESH: Lipid Peroxidation, MESH : Information Services, Antigen-Antibody Reactions, MESH: Health Education, Epitopes, MESH: Organizations, MESH: Libraries, MESH: Antigen-Antibody Reactions, lcsh:QD415-436, MESH: Animals, MESH : Organizations, MESH : Physician's Role, MESH: Bacterial Proteins, Immunosorbent Techniques, chemistry.chemical_classification, MESH: Conserved Sequence, Methodology Article, MESH : Computer Communication Networks, MESH: Chromatography, Affinity, MESH : Pseudomonas aeruginosa, MESH : Chromatography, Affinity, MESH : Immunosorbent Techniques, MESH: Ethnic Groups, MESH : Ethnic Groups, MESH: Epitopes, MESH : Patient Satisfaction, MESH : United States, MESH: Mitochondria, MESH : Antigen-Antibody Reactions, Molecular Sequence Data, MESH : Hydroxybutyrate Dehydrogenase, MESH: Sequence Alignment, Rodentia, MESH: Information Services, MESH : Epitopes, lcsh:Biochemistry, MESH : Mitochondrial Membranes, Bacterial Proteins, MESH : Conserved Sequence, Complementary DNA, MESH : Libraries, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Immunosorbent Techniques, MESH: Molecular Sequence Data, MESH: Humans, MESH : Consumer Participation, MESH : Humans, MESH: Adult, MESH: Patient Satisfaction, MESH: Hydroxybutyrate Dehydrogenase, MESH: Consumer Participation, chemistry, Lipid Peroxidation, MESH: Female, MESH: Liver, MESH : Sequence Analysis, DNA, MESH: Continental Population Groups, MESH: Sequence Analysis, DNA, MESH : Molecular Sequence Data, Dehydrogenase, Chromatography, Affinity, MESH: Mitochondrial Membranes, MESH: Antibodies, Bacterial, MESH : Bacterial Proteins, MESH : Female, MESH: Computer Communication Networks, Conserved Sequence, MESH: Aged, biology, MESH : Lipid Peroxidation, MESH : Sequence Alignment, MESH: Physician's Role, MESH : Adult, Antibodies, Bacterial, Mitochondria, Amino acid, Liver, Mitochondrial Membranes, Pseudomonas aeruginosa, MESH: Pseudomonas aeruginosa, MESH : Mitochondria, MESH : Mass Media, MESH: Mass Media, MESH : Male, Hydroxybutyrate Dehydrogenase, Affinity chromatography, MESH : Health Education, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: United States, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Antibodies, Bacterial, lcsh:QP501-801, Jaculus orientalis, MESH : Continental Population Groups, Base Sequence, MESH : Liver, Sequence Analysis, DNA, biology.organism_classification, Molecular biology, MESH: Male, Enzyme, Polyclonal antibodies, biology.protein, MESH : Base Sequence, NAD+ kinase, MESH : Animals, Sequence Alignment
Abstract

Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the enzyme. This new procedure is based on the use of polyclonal antibodies raised against BDH from bacterial Pseudomonas aeruginosa. This study improves the procedure for purification of both soluble microbial and mammalian membrane-bound BDH. Even though the Jaculus orientalis genome has not yet been sequenced, for the first time a D-3-hydroxybutyrate dehydrogenase cDNA from jerboa was cloned and sequenced. Conclusion This study applies immunoaffinity chromatography to purify BDH, the membrane-bound and lipid-dependent enzyme, as a 31 kDa single polypeptide chain. In addition, bacterial BDH isolation was achieved in a two-step purification procedure, improving the knowledge of an enzyme involved in the lipid metabolism of a unique hibernating mammal. Sequence alignment revealed conserved putative amino acids for possible NAD+ interaction.

Published
2008
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22. A PCR for the detection of mycoplasmas belonging to the Mycoplasma mycoides cluster : application to the diagnosis of contagious agalactia

Author

Lucia Manso-Silvan, François Poumarat, Marie-Pierre Pellet, François Thiaucourt, Patrice Gaurivaud, Sophie Lorenzon, V.P. Singh, Salah Woubit, Contrôle des maladies animales exotiques et émergentes ( Contrôle des maladies ), Centre de Coopération Internationale en Recherche Agronomique pour le Développement ( CIRAD ), Mycoplasmoses des ruminants [Lyon], Université de Lyon-VetAgro Sup ( VAS ), Agence Française de Sécurité Sanitaire des Aliments ( AFSSA ), AFSSA, IVRI, National Referral Lab on Mycoplasma, Contrôle des maladies animales exotiques et émergentes (Cirad-EMVT-UPR 15 Contrôle des maladies), Département Elevage et médecine vétérinaire (EMVT), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Mycoplasmoses des Ruminants - UMR (MYCO), Université de Lyon-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Agence Française de Sécurité Sanitaire des Aliments (AFSSA), and Département Elevage et médecine vétérinaire (Cirad-EMVT)

Subjects
MESH : Molecular Sequence Data, MESH : Operon, Hydrolases, Mycoplasma agalactiae, ved/biology.organism_classification_rank.species, Pcr cloning, MESH: Base Sequence, [ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, medicine.disease_cause, Polymerase Chain Reaction, Mycoplasma capricolum, Serology, 0403 veterinary science, MESH : Hydrolases, MESH: Animals, MESH: Phylogeny, MESH: Pleuropneumonia, Contagious, MESH : Polymerase Chain Reaction, Base Pairing, Phylogeny, 0303 health sciences, biology, XUMYCOPLASME, MESH : Sequence Alignment, Goats, Mycoplasma mycoides, [ SDV.SPEE ] Life Sciences [q-bio]/Santé publique et épidémiologie, 04 agricultural and veterinary sciences, 3. Good health, MESH: Hydrolases, MESH: Reproducibility of Results, MESH : Pleuropneumonia, Contagious, Milk, MESH: Mycoplasma mycoides, MESH : DNA Primers, MESH: DNA Primers, MESH: Operon, 040301 veterinary sciences, MESH: Base Pairing, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Goats, MYCOPLASME, Microbiology, 03 medical and health sciences, Operon, medicine, Animals, L50 - Physiologie et biochimie animales, Pleuropneumonia, Contagious, Molecular Biology, Gene, DNA Primers, MESH: Molecular Sequence Data, [SDV.BA.MVSA]Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal Health, Base Sequence, 030306 microbiology, ved/biology, MESH : Reproducibility of Results, MESH : Phylogeny, Reproducibility of Results, MESH: Polymerase Chain Reaction, Cell Biology, Mycoplasma, biology.organism_classification, MESH : Base Pairing, Virology, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Milk, MESH : Goats, MESH : Milk, HAFSSA, Mycoplasma putrefaciens, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, MESH : Base Sequence, MESH : Animals, [ SDV.BA.MVSA ] Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal Health, MESH : Mycoplasma mycoides, Sequence Alignment
Abstract

Contagious agalactia is a mycoplasmal infection caused by Mycoplasma agalactiae, Mycoplasma mycoides subsp. mycoides LC, M. mycoides subsp. capri, Mycoplasma capricolum subsp. capricolum and Mycoplasma putrefaciens. Identification of the causative organisms is usually performed by isolation and classical biochemical and serological tests, though this is a lengthy and cumbersome process for mycoplasmas. Specific PCR assays have been developed for the identification of Mycoplasma agalactiae and M. putrefaciens. For members of the M. mycoides cluster existing PCR tests are based on the amplification of highly conserved genes coding for ribosomal proteins, hence a possibility of cross-reactions. The gene glk, coding for a glucokinase, that is found in this cluster is very distantly related to any other bacterial glucokinase described so far. It was therefore chosen as target to design a new PCR test. The validation was performed independently in three laboratories in France and India using over 100 mycoplasma strains of various geographical origins. All strains belonging to the M. mycoides cluster were detected by amplification of the expected PCR product (428 bp) while no amplification was obtained from M. agalactiae strains. Our results demonstrate the universality of this PCR in spite of the great heterogeneity found within this cluster. This new tool may be of great help for the implementation of control measures directed towards contagious agalactia. © 2007 Elsevier Ltd All rights reserved.

Published
2007
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23. Genotyping of human cystic echinococcosis in Xinjiang, PR China

Author

Philip S. Craig, Hao Wen, M. Abdukader, Renaud Piarroux, Jean-Mathieu Bart, Ya-Lou Zhang, Minoru Nakao, Dominique-Angèle Vuitton, Akira Ito, Yunhai Wang, R. Y. Lin, Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Xinjiang Medical University, Chinese Government, Frontier Research Center for Global Change (FRCGC), Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Biomedical Sciences Research Institute, University of Salford, WHO Collaborating Center on Prevention and Treatment of Human Echinococcosis, SERF Unit, Université de Franche-Comté (UFC), Carcinogénèse épithéliale : facteurs prédictifs et pronostiques - UFC (EA 3181) (CEF2P / CARCINO), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon), Centre de Recherches Pétrographiques et Géochimiques (CRPG), Institut national des sciences de l'Univers (INSU - CNRS)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), Frontier Research Center for Global Change ( FRCGC ), Japan Agency for Marine-Earth Science and Technology ( JAMSTEC ), Université de Franche-Comté ( UFC ), Carcinogénèse épithéliale : facteurs prédictifs et pronostiques - UFC ( CEF2P / CARCINO ), Centre Hospitalier Régional Universitaire [Besançon] ( CHRU Besançon ) -Université Bourgogne Franche-Comté ( UBFC ) -Université de Franche-Comté ( UFC ), Centre de Recherches Pétrographiques et Géochimiques ( CRPG ), and Université de Lorraine ( UL ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
Veterinary medicine, MESH : Molecular Sequence Data, MESH : Aged, Helminth genetics, MESH : Child, Preschool, MESH: Base Sequence, MESH : Echinococcosis, MESH: Echinococcus granulosus, 030308 mycology & parasitology, Serology, [ SDV.CAN ] Life Sciences [q-bio]/Cancer, MESH: Dogs, 0302 clinical medicine, MESH : Dogs, MESH : Child, MESH: Child, Genotype, MESH : Genes, Helminth, MESH: Animals, Dog Diseases, Animal Husbandry, Child, Echinococcus granulosus, Genes, Helminth, MESH: Aged, Molecular Epidemiology, 0303 health sciences, MESH: Middle Aged, biology, Cysts, MESH : Sequence Alignment, MESH: Animal Husbandry, Middle Aged, MESH : Adult, MESH: China, 3. Good health, MESH : Dog Diseases, Infectious Diseases, Child, Preschool, Adult, China, Adolescent, MESH: Dog Diseases, Molecular Sequence Data, 030231 tropical medicine, Cestoda, MESH : Molecular Epidemiology, Helminthiasis, MESH: Sequence Alignment, [SDV.CAN]Life Sciences [q-bio]/Cancer, MESH : Cysts, 03 medical and health sciences, MESH: Echinococcosis, Dogs, Species Specificity, Echinococcosis, MESH : Adolescent, parasitic diseases, medicine, Animals, Humans, MESH : Species Specificity, MESH : China, MESH: Molecular Epidemiology, MESH: Species Specificity, MESH : Middle Aged, Genotyping, MESH : Animal Husbandry, Aged, MESH: Adolescent, MESH: Humans, MESH: Molecular Sequence Data, Base Sequence, Molecular epidemiology, MESH : Echinococcus granulosus, MESH : Humans, MESH: Child, Preschool, MESH: Adult, medicine.disease, biology.organism_classification, Virology, Animal Science and Zoology, Parasitology, MESH : Base Sequence, MESH : Animals, Sequence Alignment, MESH: Cysts, MESH: Genes, Helminth
Abstract

International audience; The Xinjiang Uygur Autonomous Region, multi-ethnic province in northwestern China, is one of the most important foci of human cystic echinococcosis (CE) in the world. Two Echinococcus granulosus genotypes (G1 and G6) are known to infect the intermediate hosts in this area but, to date, the source of the human infection remains unclear. The current study aimed to genetically analyse 67 hydatid cysts removed from 47 CE patients for which epidemiological, clinical and serological data were also recorded. Mitochondrial cox 1 gene sequencing suggested that the E. granulosus G1 genotype is the major source of infection (45/47 CE patients). Nevertheless, for the first time in China, 2 patients were found with hydatid cysts of the G6 genotype. In addition, 45 E. granulosus gravid tapeworms, isolated from 13 dogs, were genotyped. The majority of adult worms (42/45) exhibited the G1 genotype, whereas 3 adult tapeworms with the G6 genotype were found in one dog, that also harboured E. granulosus tapeworms of the G1 genotype. This sympatric occurrence of G1 and G6 genotypes of E. granulosus, not only in the same area but also in the same definitive host, raises the interesting question of putative genetic recombination between these E. granulosus genotypes.

Published
2006
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24. Morphological and molecular characteristics of Echinococcus multilocularis and Echinococcus granulosus mixed infection in a dog from Xinjiang, China

Author

Philip S. Craig, Hao Wen, Ya-Lou Zhang, Dominique A. Vuitton, Jean-Mathieu Bart, Patrick Giraudoux, Xinjiang Medical University, Chinese Government, Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Université de Franche-Comté ( UFC ) -Centre National de la Recherche Scientifique ( CNRS ), Biomedical Sciences Research Institute, University of Salford, WHO Collaborating Center on Prevention and Treatment of Human Echinococcosis, SERF Unit, Université de Franche-Comté ( UFC ), Carcinogénèse épithéliale : facteurs prédictifs et pronostiques - UFC ( CEF2P / CARCINO ), Centre Hospitalier Régional Universitaire [Besançon] ( CHRU Besançon ) -Université Bourgogne Franche-Comté ( UBFC ) -Université de Franche-Comté ( UFC ), Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Université de Franche-Comté (UFC), Carcinogénèse épithéliale : facteurs prédictifs et pronostiques - UFC (EA 3181) (CEF2P / CARCINO), and Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)

Subjects
Veterinary medicine, MESH : Molecular Sequence Data, MESH: Base Sequence, MESH: DNA, Helminth, MESH : Echinococcus multilocularis, MESH : Echinococcosis, MESH: Echinococcus granulosus, Polymerase Chain Reaction, 030308 mycology & parasitology, MESH: Dogs, 0302 clinical medicine, MESH : Dogs, MESH : DNA, Helminth, Genotype, MESH : Disease Reservoirs, Parasite hosting, MESH: Animals, Dog Diseases, Echinococcus granulosus, MESH: Phylogeny, MESH : Polymerase Chain Reaction, Phylogeny, 0303 health sciences, biology, MESH : RNA, Ribosomal, MESH : Sequence Alignment, General Medicine, DNA, Helminth, MESH: China, 3. Good health, MESH : Dog Diseases, PCR, MIXED INFECTION, Mitochondrial DNA, China, [ SDV.MP.PAR ] Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology, MESH: Dog Diseases, 030231 tropical medicine, Molecular Sequence Data, MESH: Sequence Alignment, Echinococcus multilocularis, CESTODE, Microbiology, 03 medical and health sciences, MESH: Echinococcosis, Dogs, Echinococcosis, parasitic diseases, Animals, MESH : China, [SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology, Gene, Disease Reservoirs, MESH: Echinococcus multilocularis, MESH: Disease Reservoirs, MESH: Molecular Sequence Data, General Veterinary, Base Sequence, MESH : Echinococcus granulosus, MESH : Phylogeny, MESH: Polymerase Chain Reaction, biology.organism_classification, Staining, Echinococcus, RNA, Ribosomal, MESH: RNA, Ribosomal, Parasitology, MESH : Base Sequence, MESH : Animals, Sequence Alignment
Abstract

International audience; The Xinjiang plateau of western China has been shown to have a high prevalence for human cystic echinococcosis (CE) caused by Echinococcus granulosus, and human alveolar echinococcosis (AE) caused by Echinococcus multilocularis. The domestic dog is suspected to be the primary definitive host for the transmission of both E. granulosus and E. multilocularis to humans in this locality. Seventeen of 30 stray dogs from Hejing County of Xinjiang were found positive for E. granulosus post mortem, and one double infection was suspected. Worm samples were collected, dyed by carmine, and observed microscopically. Carmine staining examination clearly revealed the differences in number of proglottids and appearance of uterine branches and lateral genital pore for those two species of Echinococcus. Furthermore, gene target DNA fragments were amplified for formal identification of the two parasite species, based on 12s rRNA mitochondrial gene. The PCR products were purified and sequenced. Compared with NCBI GenBank, the DNA sequences demonstrated 100% identity with E. granulosus (sheep strain, G1 genotype) and E. multilocularis.

Published
2006
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25. Role of transcription factor KLF11 and its diabetes-associated gene variants in pancreatic beta cell function

Author

Geesje M. Dallinga-Thie, Danielle Melloul, Raul Urrutia, Vered Ashkenazi-Katalan, Guillaume Charpentier, Torben Hansen, Oluf Pedersen, Nicolas Bakaher, Yamina Benmezroua, Emmanuelle Durand, Marc Prentki, Serge Hercberg, Karine Clément, Tiffany Cook, Martine Vaxillaire, Marie-Aline Charles, Valérie Delannoy, Yasmin H. Hamid, Bernadette Neve, Erik Joly, Nicole Helbecque, Christian Dina, Emmanuel Vaillant, Pilar Galan, Martin E. Fernandez-Zapico, Philippe Froguel, Hans Jansen, Institut de biologie de Lille - UMS 3702 (IBL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Mayo Clinic [Rochester], Hadassah Hebrew University Medical Center [Jerusalem], Génétique des maladies multifactorielles (GMM), Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique (CNRS), Steno Diabetes Center and Hagedorn Research Institute, Departement /u563 : Immunologie et Maladies infectieuses, Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Réponse immunitaire et complexe majeur d'histocompatibilité (U395), Institut National de la Santé et de la Recherche Médicale (INSERM), Departement /u563 : Lipoproteines et Mediateurs Lipidiques, Erasmus University Medical Center [Rotterdam] (Erasmus MC), Recherche en épidémiologie et biostatistique, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Systèmes Macromoléculaires et Physiopathologie Humaine (SMPH), BIOMERIEUX-Centre National de la Recherche Scientifique (CNRS), Epidémiologie cardiovasculaire et métabolique, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Déterminants Biologiques et Comportementaux des Obésités, EA3502-Hôtel-Dieu-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Pierre et Marie Curie - Paris 6 (UPMC), Service de nutrition, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital de l'Hôtel-Dieu, Nutrition et obésité : approches génétique et transcriptomique, Université Pierre et Marie Curie - Paris 6 (UPMC)-IFR58-Institut National de la Santé et de la Recherche Médicale (INSERM), Département de nutrition, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôtel-Dieu, Unité de Recherche en Epidémiologie Nutritionnelle (UREN), Université Paris 13 (UP13)-Institut National de la Recherche Agronomique (INRA)-Conservatoire National des Arts et Métiers [CNAM] (CNAM)-Université Sorbonne Paris Cité (USPC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epidémiologie des maladies chroniques: impact des intéractions gène environnement sur la santé des populations, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Centre Hospitalier Sud Francilien, CH Evry-Corbeil, Hopital Notre-Dame, Steno Diabetes Center, Section of Genomic Medicine, Imperial College London, Genome Centre, Imperial College London-Hammersmith campus, Centre de Physiopathologie Toulouse Purpan ex IFR 30 et IFR 150 (CPTP), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), The Functional Immunogenetics Laboratory, The Babraham Institute, Institut de Chimie de la Matière Condensée de Bordeaux (ICMCB), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Développement artériel, Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Mercator Océan, Société Civile CNRS Ifremer IRD Météo-France SHOM, EA3502-Hôtel-Dieu-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Pierre et Marie Curie - Paris 6 (UPMC), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital de l'Hôtel-Dieu, Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôtel-Dieu, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Sorbonne Paris Cité (USPC)-Université Paris 13 (UP13)-Conservatoire National des Arts et Métiers [CNAM] (CNAM)-Institut National de la Recherche Agronomique (INRA), Epidémiologie des maladies chroniques : impact des interactions gène environnement sur la santé des populations, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé, Service de diabétologie, CH Evry-Corbeil-CH Evry-Corbeil, Service d'endocrinologie et diabetologie, Hôpital de Corbeil-ESsonnes, Génétique des maladies multifactorielles ( GMM ), Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique ( CNRS ), Centre de Physiopathologie Toulouse Purpan (ex IFR 30 et IFR 150), Université Toulouse III - Paul Sabatier ( UPS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR30-IFR150-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Toulouse III - Paul Sabatier ( UPS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR30-IFR150-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Réponse immunitaire et complexe majeur d'histocompatibilité ( U395 ), Institut National de la Santé et de la Recherche Médicale ( INSERM ), Physique, Université de Lille, Sciences Humaines et Sociales, Institut de Chimie de la Matière Condensée de Bordeaux ( ICMCB ), Centre National de la Recherche Scientifique ( CNRS ) -Université de Bordeaux ( UB ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Université Paris-Sud - Paris 11 ( UP11 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Systèmes Macromoléculaires et Physiopathologie Humaine ( SMPH ), BIOMERIEUX-Centre National de la Recherche Scientifique ( CNRS ), EA3502-Hôtel-Dieu-Assistance publique - Hôpitaux de Paris (AP-HP)-Université Pierre et Marie Curie - Paris 6 ( UPMC ), Assistance publique - Hôpitaux de Paris (AP-HP)-Hôpital de l'Hôtel-Dieu, Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IFR58-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Assistance publique - Hôpitaux de Paris (AP-HP)-Hôtel-Dieu, Unité de Recherche en Epidémiologie Nutritionnelle ( UREN ), Institut National de la Recherche Agronomique ( INRA ) -Conservatoire National des Arts et Métiers [CNAM] ( CNAM ) -Université Paris 13 ( UP13 ) -Université Sorbonne Paris Cité ( USPC ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Réseau International des Instituts Pasteur ( RIIP ) -Réseau International des Instituts Pasteur ( RIIP ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Lille, Droit et Santé-Centre Hospitalier Régional Universitaire [Lille] ( CHRU Lille ), Réseau International des Instituts Pasteur ( RIIP ) -Réseau International des Instituts Pasteur ( RIIP ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Lille, Droit et Santé, Department of Applied Physics ( GU ), State University of Ghent, Vascular Medicine, Experimental Vascular Medicine, Université Pierre et Marie Curie - Paris 6 (UPMC)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôtel-Dieu-EA3502, Université Paris 13 (UP13)-Institut National de la Recherche Agronomique (INRA)-Conservatoire National des Arts et Métiers [CNAM] (CNAM), HESAM Université (HESAM)-HESAM Université (HESAM)-Université Sorbonne Paris Cité (USPC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Internal Medicine, Clinical Chemistry, Centre National de la Recherche Scientifique (CNRS)-Université de Bordeaux (UB), Université Pierre et Marie Curie - Paris 6 (UPMC)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôtel-Dieu-EA3502, Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-Université Sorbonne Paris Cité (USPC)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
medicine.medical_treatment, Cell Cycle Proteins, MESH: Base Sequence, 0302 clinical medicine, MESH : Cell Cycle Proteins, Human genetics, Insulin, MESH: Gene Components, [ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human genetics, Regulation of gene expression, MESH: Chromatin Immunoprecipitation, 0303 health sciences, Base Composition, MESH : Gene Expression Regulation, MESH: Transcription Factors, MESH: Case-Control Studies, 3. Good health, Pedigree, MESH: Promoter Regions (Genetics), MESH: Repressor Proteins, Promoter Regions (Genetics), Pancreas, Type 2, MESH: Diabetes Mellitus, Type 2, MESH : Case-Control Studies, MESH: Pedigree, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Insulin, 03 medical and health sciences, Islets of Langerhans, MESH: Cell Cycle Proteins, SDG 3 - Good Health and Well-being, Genetic, MESH: Polymorphism, Genetic, Diabetes Mellitus, Humans, MESH : Islets of Langerhans, Polymorphism, Polymorphism, Genetic, MESH: Humans, MESH: Molecular Sequence Data, MESH: Islets of Langerhans, MESH : Humans, DNA, medicine.disease, MESH : Promoter Regions (Genetics), Diabetes Mellitus, Type 2, Case-Control Studies, MESH: Luciferases, Apoptosis Regulatory Proteins, MESH : Sequence Analysis, DNA, Transcription Factors, MESH: Sequence Analysis, DNA, MESH : Molecular Sequence Data, MESH : Transcription Factors, MESH : Polymorphism, Genetic, MESH : Insulin, Type 2 diabetes, MESH : Diabetes Mellitus, Type 2, Promoter Regions, Genetic, Luciferases, Multidisciplinary, MESH : Sequence Alignment, Biological Sciences, MESH : Gene Components, MESH: Gene Expression Regulation, Europe, medicine.anatomical_structure, Gene Components, Base Sequence, Chromatin Immunoprecipitation, Gene Expression Regulation, Repressor Proteins, Sequence Alignment, Sequence Analysis, Beta cell, MESH : Repressor Proteins, MESH : Europe, 030209 endocrinology & metabolism, Biology, MESH : Base Composition, Génétique humaine, MESH : Chromatin Immunoprecipitation, MESH: Base Composition, Diabetes mellitus, medicine, Transcription factor, 030304 developmental biology, MESH : Luciferases, Type 2 Diabetes Mellitus, Sequence Analysis, DNA, Molecular biology, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, MESH : Pedigree, MESH : Base Sequence, MESH: Europe
Abstract

KLF11 (TIEG2) is a pancreas-enriched transcription factor that has elicited significant attention because of its role as negative regulator of exocrine cell growth in vitro and in vivo . However, its functional role in the endocrine pancreas remains to be established. Here, we report, for the first time, to our knowledge, the characterization of KLF11 as a glucose-inducible regulator of the insulin gene. A combination of random oligonucleotide binding, EMSA, luciferase reporter, and chromatin immunoprecipitation assays shows that KLF11 binds to the insulin promoter and regulates its activity in beta cells. Genetic analysis of the KLF11 gene revealed two rare variants (Ala347Ser and Thr220Met) that segregate with diabetes in families with early-onset type 2 diabetes, and significantly impair its transcriptional activity. In addition, analysis of 1,696 type 2 diabetes mellitus and 1,776 normoglycemic subjects show a frequent polymorphic Gln62Arg variant that significantly associates with type 2 diabetes mellitus in North European populations (OR = 1.29, P = 0.00033). Moreover, this variant alters the corepressor mSin3A-binding activity of KLF11, impairs the activation of the insulin promoter and shows lower levels of insulin expression in pancreatic beta cells. In addition, subjects carrying the Gln62Arg allele show decreased plasma insulin after an oral glucose challenge. Interestingly, all three nonsynonymous KLF11 variants show increased repression of the catalase 1 promoter, suggesting a role in free radical clearance that may render beta cells more sensitive to oxidative stress. Thus, both functional and genetic analyses reveal that KLF11 plays a role in the regulation of pancreatic beta cell physiology, and its variants may contribute to the development of diabetes.

Published
2005
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26. Apisalpha2, Apisalpha7-1 and Apisalpha7-2: three new neuronal nicotinic acetylcholine receptor alpha-subunits in the honeybee brain

Author

Thany, S. H., Crozatier, M., Raymond-Delpech, V., Gauthier, Mélanie, Lenaers, G., Laboratoire Récepteurs et Canaux Ioniques Membranaires ( RCIM ), Université d'Angers ( UA ) -Institut National de la Recherche Agronomique ( INRA ), Centre de biologie du développement ( CBD ), Université Toulouse III - Paul Sabatier ( UPS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique ( CNRS ), Centre de Recherches sur la Cognition Animale ( CRCA ), Université Paris Descartes - Paris 5 ( UPD5 ), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) ( FEMTO-ST ), Université de Franche-Comté ( UFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Université de Technologie de Belfort-Montbeliard ( UTBM ), Institut de minéralogie et de physique des milieux condensés ( IMPMC ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IPG PARIS-Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut fur Biologie, AG Neurobiologie, Freie Universität Berlin [Berlin], Laboratoire d'automatique de Besançon ( LAB ), Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), Institut FRESNEL ( FRESNEL ), Aix Marseille Université ( AMU ) -Ecole Centrale de Marseille ( ECM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération ( LBCMCP ), Physiopathologie et thérapie des déficits sensoriels et moteurs, Université Montpellier 2 - Sciences et Techniques ( UM2 ) -IFR76-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Récepteurs et Canaux Ioniques Membranaires (RCIM), Université d'Angers (UA)-Institut National de la Recherche Agronomique (INRA), Centre de biologie du développement (CBD), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur la Cognition Animale (CRCA), Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut des sciences du cerveau de Toulouse. (ISCT), Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J)-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie et de physique des milieux condensés (IMPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Freie Universität Berlin, Laboratoire d'automatique de Besançon (LAB), Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Institut FRESNEL (FRESNEL), Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU), Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Montpellier 2 - Sciences et Techniques (UM2)-IFR76-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Récepteurs et Canaux Ioniques Membranaires (RCIM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Institut des sciences du cerveau de Toulouse. (ISCT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM), Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur la Cognition Animale - UMR5169 (CRCA), Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Physique du Globe de Paris (IPG Paris)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Sequence Analysis, DNA, MESH : RNA, Messenger, MESH : Molecular Sequence Data, MESH: Sequence Homology, Amino Acid, MESH : DNA, Complementary, MESH: Neurons, Gene Expression, Genes, Insect, MESH: Amino Acid Sequence, MESH: Genes, Insect, Receptors, Nicotinic, MESH: Bees, MESH : Bees, MESH: Reverse Transcriptase Polymerase Chain Reaction, MESH: Animals, MESH: Phylogeny, In Situ Hybridization, Phylogeny, Neurons, Reverse Transcriptase Polymerase Chain Reaction, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH : Reverse Transcriptase Polymerase Chain Reaction, MESH : Genes, Insect, Brain, MESH : In Situ Hybridization, Bees, MESH : Sequence Homology, Amino Acid, Multigene Family, MESH: Receptors, Nicotinic, DNA, Complementary, MESH: Gene Expression, Molecular Sequence Data, MESH: Sequence Alignment, MESH : Multigene Family, MESH : Neurons, MESH: Brain, MESH: In Situ Hybridization, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, RNA, Messenger, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: RNA, Messenger, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, MESH : Receptors, Nicotinic, MESH : Phylogeny, Sequence Analysis, DNA, MESH: DNA, Complementary, MESH : Gene Expression, MESH : Brain, MESH: Multigene Family, MESH : Animals, Sequence Alignment, MESH : Sequence Analysis, DNA
Abstract

Acetylcholine is the principal excitatory neurotransmitter in the central nervous system of insects. Nicotinic acetylcholine receptors, which belong to the ligand-gated ion channel family, constitute important targets for insecticides. In the honeybee Apis mellifera, pharmacological evidence supports the existence of several nicotinic acetylcholine receptors. In this paper, we report the identification of three new genes that encode nicotinic acetylcholine receptor alpha-subunits in the honeybee. Phylogenetic comparisons with other ligand-gated ion channel subunit sequences support their classification as Apisalpha2, Apisalpha7-1 and Apisalpha7-2 subunits. Based on in situ hybridization experiments, we determined their expression patterns in the different brain regions of pupae and adult honeybees. Our results show that these nicotinic acetylcholine receptor subunits are differently expressed among the brain regions and that they appear at different stages of honeybee development.

Published
2005
Full Text
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27. Identification and localization of the nicotinic acetylcholine receptor alpha3 mRNA in the brain of the honeybee, Apis mellifera

Author

Steeve H. Thany, Mélanie Gauthier, Catherine Armengaud, Guy Lenaers, M. Crozatier, Récepteurs et Canaux Ioniques Membranaires (RCIM), Université d'Angers (UA)-Institut National de la Recherche Agronomique (INRA), Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et thérapie des déficits sensoriels et moteurs, Université Montpellier 2 - Sciences et Techniques (UM2)-IFR76-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de biologie du développement (CBD), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Centre de Recherches sur la Cognition Animale - UMR5169 (CRCA), Institut des sciences du cerveau de Toulouse. (ISCT), Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Paris Descartes - Paris 5 (UPD5), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Institut de minéralogie et de physique des milieux condensés (IMPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Physique du Globe de Paris (IPG Paris)-Centre National de la Recherche Scientifique (CNRS), Institut fur Biologie, AG Neurobiologie, Freie Universität Berlin, Laboratoire d'automatique de Besançon (LAB), Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Institut FRESNEL (FRESNEL), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Récepteurs et Canaux Ioniques Membranaires (RCIM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Centre de Recherches sur la Cognition Animale (CRCA), Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM), Université Pierre et Marie Curie - Paris 6 (UPMC)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Récepteurs et Canaux Ioniques Membranaires ( RCIM ), Université d'Angers ( UA ) -Institut National de la Recherche Agronomique ( INRA ), Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération ( LBCMCP ), Université Toulouse III - Paul Sabatier ( UPS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique ( CNRS ), Université Montpellier 2 - Sciences et Techniques ( UM2 ) -IFR76-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Centre de biologie du développement ( CBD ), Centre de Recherches sur la Cognition Animale ( CRCA ), Université Paris Descartes - Paris 5 ( UPD5 ), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) ( FEMTO-ST ), Université de Franche-Comté ( UFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Université de Technologie de Belfort-Montbeliard ( UTBM ), Institut de minéralogie et de physique des milieux condensés ( IMPMC ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IPG PARIS-Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Freie Universität Berlin [Berlin], Laboratoire d'automatique de Besançon ( LAB ), Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), Institut FRESNEL ( FRESNEL ), Aix Marseille Université ( AMU ) -Ecole Centrale de Marseille ( ECM ) -Centre National de la Recherche Scientifique ( CNRS ), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre de Biologie Intégrative (CBI), Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut des sciences du cerveau de Toulouse. (ISCT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J)-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Haenlin, Marc

Subjects
MESH : RNA, Messenger, MESH : Molecular Sequence Data, MESH : DNA, MESH: Amino Acid Sequence, Receptors, Nicotinic, MESH: Base Sequence, Polymerase Chain Reaction, MESH: Bees, MESH : Bees, 0302 clinical medicine, Ganglion type nicotinic receptor, MESH: Animals, Cloning, Molecular, MESH: Phylogeny, MESH : Polymerase Chain Reaction, In Situ Hybridization, Phylogeny, G alpha subunit, 0303 health sciences, MESH : Gene Expression Regulation, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH: DNA, Brain, MESH : In Situ Hybridization, Bees, MESH: Gene Expression Regulation, 3. Good health, Cell biology, Nicotinic acetylcholine receptor, Nicotinic agonist, Biochemistry, Mushroom bodies, MESH: Receptors, Nicotinic, MESH : Cloning, Molecular, Molecular Sequence Data, MESH: Sequence Alignment, In situ hybridization, Neurotransmission, Biology, 03 medical and health sciences, MESH: Brain, MESH: In Situ Hybridization, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Genetics, Animals, MESH: Cloning, Molecular, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, RNA, Messenger, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, Acetylcholine receptor, MESH: RNA, Messenger, MESH: Molecular Sequence Data, Base Sequence, MESH : Receptors, Nicotinic, MESH : Phylogeny, MESH: Polymerase Chain Reaction, DNA, Gene Expression Regulation, MESH : Brain, Insect Science, MESH : Base Sequence, MESH : Animals, Sequence Alignment, 030217 neurology & neurosurgery
Abstract

The nicotinic acetylcholine receptors are ligand-gated ion channels responsible for rapid neurotransmission and are target sites for pesticides in insects. In the honeybee Apis mellifera, pharmacological and electrophysiological studies have shown that different nicotinic acetylcholine receptor subtypes may exist in the brain. Here, we have identified a honeybee cDNA that encodes a 537 amino acid protein with features typical of nicotinic acetylcholine receptor alpha subunit, and sequence homology to human alpha3. In situ hybridization on cryosections shows that the Apisalpha3 mRNA is differently expressed in larvae and adult. In larvae, Apisalpha3 mRNA expression is restricted to the suboesophageal ganglia. In adult, it is further expressed in the optic lobes, the dorsal lobes, the antennal lobes and the calyces of mushroom bodies. Together our results suggest that Apisalpha3 shows a controlled expression pattern during development.

Published
2003

28. Cloning and characterization of the human and rat islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP) genes

Author

Philippe Froguel, Claudia Frigeri, James K. Oeser, Christina A. Svitek, Richard M. O'Brien, Randall Wong, Joshua K. Goldman, Lauri A. Hornbuckle, Larry J. Bischof, David Wahl, John C. Hutton, Barbara Bergman, Cyrus C. Martin, Frédéric Leprêtre, Carl Hilliker, Informatique et Distribution (ID-IMAG), Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Physique des interactions ioniques et moléculaires (PIIM), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Laboratoire de cristallographie et sciences des matériaux (CRISMAT), École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC), California Institute of Technology (CALTECH), Sol Agro et hydrosystème Spatialisation (SAS), AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de la Recherche Agronomique (INRA), Laboratoire d'électrotechnique de Grenoble (LEG), Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG), Laboratoire de rhéologie (LR), Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Grenoble (INPG)-Université Joseph Fourier - Grenoble 1 (UJF), Institut de Recherches Historiques du Septentrion (IRHiS) - UMR 8529 (IRHiS), Centre National de la Recherche Scientifique (CNRS)-Université de Lille, Laboratoire d'Astrophysique de Marseille (LAM), Aix Marseille Université (AMU)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National d'Études Spatiales [Toulouse] (CNES)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de catalyse de Lille - UMR 8010 (LCL), Université de Lille, Sciences et Technologies-Centrale Lille-Centre National de la Recherche Scientifique (CNRS), Unité de Catalyse et Chimie du Solide - UMR 8181 (UCCS), Centrale Lille Institut (CLIL)-Université d'Artois (UA)-Centrale Lille-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Lille, Domaines Océaniques (LDO), Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Observatoire des Sciences de l'Univers-Institut d'écologie et environnement-Centre National de la Recherche Scientifique (CNRS), Génétique médicale et fonctionnelle du cancer et des maladies neuropsychiatriques, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de génétique [Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Études des Structures, des Processus d’Adaptation et des Changements de l’Espace (ESPACE ), Université de la Méditerranée - Aix-Marseille 2-Université de Provence - Aix-Marseille 1-Avignon Université (AU)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Université de Nice Sophia-Antipolis (UNSA), Synchrotron Radiation Source (SRS), CCLRC Daresbury Laboratory, Institut de Mathématiques de Bourgogne [Dijon] (IMB), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Bourgogne (UB), Université de Bourgogne (UB), Science et Ingénierie des Matériaux et Procédés (SIMaP), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National Polytechnique de Grenoble (INPG)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Génie des procédés papetiers (LGP2 ), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Génie Electrique de Grenoble (G2ELab), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Centre National de la Recherche Scientifique (CNRS), Department of Human Genetics, Emory University [Atlanta, GA], Neurosciences Sensorielles Comportement Cognition, Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Unité de Médecine Interne Thrombose Maladies Vasculaires, Nouvelles Approches Anti-Thrombotiques, Université Henri Poincaré - Nancy 1 (UHP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génétique des maladies multifactorielles (GMM), Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique (CNRS), Section of Genomic Medicine, Imperial College London, Genome Centre, Imperial College London-Hammersmith campus, Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Université de Caen Normandie (UNICAEN), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Aix Marseille Université (AMU)-Centre National d'Études Spatiales [Toulouse] (CNES), Laboratoire de catalyse de Lille (LCL), Université de Lille, Sciences et Technologies-Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille (ENSCL)-Centre National de la Recherche Scientifique (CNRS), Unité de Catalyse et de Chimie du Solide - UMR 8181 (UCCS), Université d'Artois (UA)-Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille (ENSCL)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Laboratoire Génie des procédés papetiers (LGP2), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche sur les Matériaux Avancés (IRMA), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université d'Artois (UA)-Centrale Lille-Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Informatique et Distribution ( ID-IMAG ), Institut National de Recherche en Informatique et en Automatique ( Inria ) -Institut National Polytechnique de Grenoble ( INPG ) -Centre National de la Recherche Scientifique ( CNRS ), Physique des interactions ioniques et moléculaires ( PIIM ), Aix Marseille Université ( AMU ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de cristallographie et sciences des matériaux ( CRISMAT ), Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure d'Ingénieurs de Caen ( ENSICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ) -Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ), California Institute of Technology ( CALTECH ), Sol Agro et hydrosystème Spatialisation ( SAS ), Institut National de la Recherche Agronomique ( INRA ) -AGROCAMPUS OUEST, Laboratoire d'électrotechnique de Grenoble ( LEG ), Institut National Polytechnique de Grenoble ( INPG ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de rhéologie ( LR ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut National Polytechnique de Grenoble ( INPG ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Recherches Historiques du Septentrion (IRHiS) - UMR 8529 ( IRHiS ), Université de Lille-Centre National de la Recherche Scientifique ( CNRS ), Laboratoire d'Astrophysique de Marseille ( LAM ), Centre National de la Recherche Scientifique ( CNRS ) -Institut national des sciences de l'Univers ( INSU - CNRS ) -Aix Marseille Université ( AMU ) -Centre National d'Etudes Spatiales ( CNES ), Laboratoire de catalyse de Lille ( LCL ), Université de Lille, Sciences et Technologies-Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille ( ENSCL ) -Centre National de la Recherche Scientifique ( CNRS ), Unité de Catalyse et de Chimie du Solide - UMR 8181 ( UCCS ), Université d'Artois ( UA ) -Ecole Centrale de Lille-Ecole Nationale Supérieure de Chimie de Lille ( ENSCL ) -Université de Lille-Centre National de la Recherche Scientifique ( CNRS ), Domaines Océaniques ( LDO ), Centre National de la Recherche Scientifique ( CNRS ) -Institut d'écologie et environnement-Observatoire des Sciences de l'Univers-Université de Brest ( UBO ) -Institut national des sciences de l'Univers ( INSU - CNRS ), Université de Rouen Normandie ( UNIROUEN ), Normandie Université ( NU ) -Normandie Université ( NU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), CHU Rouen-Université de Rouen Normandie ( UNIROUEN ), Normandie Université ( NU ) -Normandie Université ( NU ), Études des Structures, des Processus d’Adaptation et des Changements de l’Espace ( ESPACE ), Université Nice Sophia Antipolis ( UNS ), Université Côte d'Azur ( UCA ) -Université Côte d'Azur ( UCA ) -Université d'Avignon et des Pays de Vaucluse ( UAPV ) -Aix Marseille Université ( AMU ) -Centre National de la Recherche Scientifique ( CNRS ), Institut des Sciences de l'Evolution de Montpellier ( ISEM ), Université de Montpellier ( UM ) -Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique ( CNRS ), Synchrotron Radiation Source ( SRS ), Institut de Mathématiques de Bourgogne [Dijon] ( IMB ), Université de Bourgogne ( UB ) -Centre National de la Recherche Scientifique ( CNRS ), Université de Bourgogne ( UB ), Science et Ingénierie des Matériaux et Procédés ( SIMaP ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut polytechnique de Grenoble - Grenoble Institute of Technology ( Grenoble INP ) -Institut National Polytechnique de Grenoble ( INPG ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Centre de Recherches sur l'Action Politique en Europe ( ARENES ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Institut d'Études Politiques [IEP] - Rennes-École des Hautes Études en Santé Publique [EHESP] ( EHESP ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire Génie des procédés papetiers ( LGP2 ), Centre Technique du Papier ( CTP ) -Institut National Polytechnique de Grenoble ( INPG ) -École Française de Papeterie et des Industries Graphiques-Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Génie Electrique de Grenoble ( G2ELab ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut polytechnique de Grenoble - Grenoble Institute of Technology ( Grenoble INP ) -Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Université Henri Poincaré - Nancy 1 ( UHP ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Génétique des maladies multifactorielles ( GMM ), Université de Lille, Droit et Santé-Centre National de la Recherche Scientifique ( CNRS ), and Laboratoire de thermodynamique et physico-chimie métallurgiques (LTPCM)

Subjects
MESH : Molecular Sequence Data, MESH : RNA, Messenger, Messenger, MESH: Catalytic Domain, MESH: Amino Acid Sequence, MESH : Glucose-6-Phosphatase, MESH: Base Sequence, Biochemistry, Conserved sequence, MESH : Proteins, Immunoenzyme Techniques, Mice, 0302 clinical medicine, Human genetics, Catalytic Domain, MESH: Reverse Transcriptase Polymerase Chain Reaction, Gene expression, Coding region, MESH: Animals, MESH: Proteins, Cloning, Molecular, [ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human genetics, Promoter Regions, Genetic, Peptide sequence, Conserved Sequence, 0303 health sciences, MESH: Conserved Sequence, biology, MESH : Rats, Reverse Transcriptase Polymerase Chain Reaction, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH : Reverse Transcriptase Polymerase Chain Reaction, MESH : Catalytic Domain, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Glucose-6-Phosphatase, Humans, Molecular Sequence Data, Promoter Regions (Genetics), Proteins, RNA, Rats, Sequence Alignment, MESH: Promoter Regions (Genetics), Glucose 6-phosphatase, endocrine system, MESH : Cloning, Molecular, MESH: Rats, G6PC2, TATA box, MESH: Sequence Alignment, 030209 endocrinology & metabolism, 03 medical and health sciences, Génétique humaine, MESH : Conserved Sequence, MESH : Immunoenzyme Techniques, MESH : Mice, MESH: Cloning, Molecular, RNA, Messenger, MESH: Immunoenzyme Techniques, Molecular Biology, Gene, MESH: Mice, 030304 developmental biology, MESH: RNA, Messenger, MESH: Humans, MESH: Molecular Sequence Data, MESH : Humans, Cell Biology, MESH : Promoter Regions (Genetics), Molecular biology, MESH: Glucose-6-Phosphatase, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, biology.protein, MESH : Base Sequence, MESH : Animals
Abstract

Islet-specific glucose-6-phosphatase (G6Pase) catalytic subunit-related protein (IGRP) is a homolog of the catalytic subunit of G6Pase, the enzyme that catalyzes the terminal step of the gluconeogenic pathway. Its catalytic activity, however, has not been defined. Since IGRP gene expression is restricted to islets, this suggests a possible role in the regulation of islet metabolism and, hence, insulin secretion induced by metabolites. We report here a comparative analysis of the human, mouse, and rat IGRP genes. These studies aimed to identify conserved sequences that may be critical for IGRP function and that specify its restricted tissue distribution. The single copy human IGRP gene has five exons of similar length and coding sequence to the mouse IGRP gene and is located on human chromosome 2q28-32 adjacent to the myosin heavy chain 1B gene. In contrast, the rat IGRP gene does not appear to encode a protein as a result of a series of deletions and insertions in the coding sequence. Moreover, rat IGRP mRNA, unlike mouse and human IGRP mRNA, is not expressed in islets or islet-derived cell lines, an observation that was traced by fusion gene analysis to a mutation of the TATA box motif in the mouse/human IGRP promoters to TGTA in the rat sequence. The results provide a framework for the further analysis of the molecular basis for the tissue-restricted expression of the IGRP gene and the identification of key amino acid sequences that determine its biological activity.

Published
2001
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29. Evidence for an uncommon alpha-actinin protein in Trichomonas vaginalis

Author

Gérard Coffe, Geneviève Bricheux, Guy Brugerolle, Nathalie Pradel, Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA), Laboratoire de Biologie des Protistes [Aubière] (LBP), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Microorganismes : Génome et Environnement ( LMGE ), Université Blaise Pascal - Clermont-Ferrand 2 ( UBP ) -Université d'Auvergne - Clermont-Ferrand I ( UdA ) -Centre National de la Recherche Scientifique ( CNRS ), BRICHEUX, Genevieve, and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Trichomonas vaginalis, MESH : Molecular Sequence Data, Transcription, Genetic, MESH : DNA, Complementary, Fluorescent Antibody Technique, MESH : Actins, MESH: Protein Structure, Secondary, MESH : Blotting, Western, Actinin, MESH: Amino Acid Sequence, MESH: Base Sequence, Protein Structure, Secondary, Homology (biology), MESH : Cytoskeleton, Protein sequencing, MESH: Actinin, Electrophoresis, Gel, Two-Dimensional, MESH: Animals, Peptide sequence, MESH: Fluorescent Antibody Technique, Cytoskeleton, MESH : Consensus Sequence, MESH : Sequence Alignment, MESH : Amino Acid Sequence, MESH : Blotting, Northern, [ SDV.MP.PRO ] Life Sciences [q-bio]/Microbiology and Parasitology/Protistology, Actinin, alpha 1, Biochemistry, MESH: Calcium, MESH: 5' Untranslated Regions, Electrophoresis, Polyacrylamide Gel, DNA, Complementary, Blotting, Western, Molecular Sequence Data, MESH: Sequence Alignment, Sequence alignment, macromolecular substances, [SDV.MP.PRO] Life Sciences [q-bio]/Microbiology and Parasitology/Protistology, Biology, MESH : Electrophoresis, Polyacrylamide Gel, MESH: Actins, [SDV.MP.PRO]Life Sciences [q-bio]/Microbiology and Parasitology/Protistology, Consensus Sequence, Trichomonas vaginalis, Consensus sequence, MESH: Cytoskeleton, Animals, MESH: Blotting, Northern, MESH: Blotting, Western, Amino Acid Sequence, MESH: Consensus Sequence, MESH : Calcium, Molecular Biology, Actin, MESH: Molecular Sequence Data, Base Sequence, MESH: Transcription, Genetic, MESH : 5' Untranslated Regions, MESH : Transcription, Genetic, MESH : Electrophoresis, Gel, Two-Dimensional, MESH: DNA, Complementary, MESH : Trichomonas vaginalis, Blotting, Northern, MESH: Electrophoresis, Gel, Two-Dimensional, Molecular biology, Actins, MESH : Fluorescent Antibody Technique, Calcium, MESH : Base Sequence, Parasitology, MESH : Protein Structure, Secondary, MESH : Animals, 5' Untranslated Regions, Sequence Alignment, MESH : Actinin, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; As part of our ongoing project of identification of actin-binding proteins implicated in the cell transition (flagellate to amoeboid/adherent) of Trichomonas vaginalis, we have characterized an alpha-actinin-related protein in this parasite. The protein (P100) has a molecular mass of 100 kDa and an isoelectric point of 5.5. A monoclonal antibody raised against this protein co-localizes with the actin network. P100 gene transcripts are co-expressed with actin throughout the cell cycle. Analysis of the deduced protein sequence reveals three domains: an N-terminal actin-binding region; a central region rich in alpha-helix; and a C-terminal domain with Ca(2+)-binding capacity. Whereas the N- and C-terminal regions are well-conserved as compared to other alpha-actinins, we observe in the central region an atypical distribution of residues in five repeats. The sequence of the repeats does not show any homology with the rod domain of the other alpha-actinins, except for the first repeat which shows some similarity. The four other repeats of T. vaginalis P100 appear to result from a duplication event which is not detectable in the other sequences.

Published
1998

30. A 1,3-beta-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus is a homologue of the yeast Bgl2p

Author

Mouyna , Isabelle, Hartland , Robbert P., Fontaine , Thierry, Diaquin , Michel, Simenel , Catherine, Delepierre , Murielle, Henrissat , Bernard, Latgé , Jean-Paul, Aspergillus, Institut Pasteur [Paris], Résonance Magnétique Nucléaire, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique ( CNRS ), Architecture et fonction des macromolécules biologiques ( AFMB ), Centre National de la Recherche Scientifique ( CNRS ) -Aix Marseille Université ( AMU ) -Institut National de la Recherche Agronomique ( INRA ), and The authors thank J. d’Alayer for performing the amino acid sequencing and J. Lemoine for the matrix-assisted de- sorption/time-of-flight mass spectrometry analysis. I. Mouyna and R. Hartland made equal contributions to the work published.

Subjects
MESH : Chromatography, Ion Exchange, MESH : Molecular Sequence Data, MESH : Cloning, Molecular, MESH : Candida albicans, MESH : Amino Acid Sequence, MESH : Sequence Alignment, MESH : Glucan Endo-1,3-beta-D-Glucosidase, MESH : Saccharomyces cerevisiae, MESH : Sequence Homology, Amino Acid, MESH : Saccharomyces cerevisiae Proteins, MESH : Aspergillus fumigatus, MESH : Genes, Fungal, MESH : DNA, Fungal, MESH : Transformation, Genetic, skin and connective tissue diseases, [ SDV.MP.MYC ] Life Sciences [q-bio]/Microbiology and Parasitology/Mycology, MESH : Sequence Analysis, DNA, MESH : Cell Wall
Abstract

International audience; A 1,3-beta-glucanosyltransferase which introduces intrachain 1,6-beta linkages into 1,3-beta-glucan was isolated from the cell wall of Aspergillus fumigatus. The biochemical and molecular characterization of the A. fumigatus transferase showed it was homologous to the Saccharomyces cerevisiae and Candida albicans transferase Bgl2p. A null mutant constructed in A. fumigatus by gene replacement did not show a distinct phenotype from the parental strain. The putative function of this major cell-wall-associated protein is discussed.

Published
1998
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