Author: "Pascal Cosette" / Topic: medicine - Searchworks@Jio Institute Digital Library Search Results

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1. Gingival proteomics reveals the role of TGF beta and YAP/TAZ signaling in Raine syndrome fibrosis

Author: Cláudio Rodrigues Rezende Costa, Rym Chalgoumi, Amina Baker, Clément Guillou, Paulo Marcio Yamaguti, Victor Simancas Escorcia, Lilia Abbad, Bruna Rabelo Amorin, Caroline Lourenço de Lima, Vidjea Cannaya, Mourad Benassarou, Ariane Berdal, Christos Chatziantoniou, Olivier Cases, Pascal Cosette, Renata Kozyraki, and Ana Carolina Acevedo
Subjects: FAM20C, FAM20A, Secretome, Proteome, Raine syndrome, TGF beta, Medicine, Science
Abstract: Abstract Raine syndrome (RNS) is a rare autosomal recessive osteosclerotic dysplasia. RNS is caused by loss-of-function disease-causative variants of the FAM20C gene that encodes a kinase that phosphorylates most of the secreted proteins found in the body fluids and extracellular matrix. The most common RNS clinical features are generalized osteosclerosis, facial dysmorphism, intracerebral calcifications and respiratory defects. In non-lethal RNS forms, oral traits include a well-studied hypoplastic amelogenesis imperfecta (AI) and a much less characterized gingival phenotype. We used immunomorphological, biochemical, and siRNA approaches to analyze gingival tissues and primary cultures of gingival fibroblasts of two unrelated, previously reported RNS patients. We showed that fibrosis, pathological gingival calcifications and increased expression of various profibrotic and pro-osteogenic proteins such as POSTN, SPARC and VIM were common findings. Proteomic analysis of differentially expressed proteins demonstrated that proteins involved in extracellular matrix (ECM) regulation and related to the TGFβ/SMAD signaling pathway were increased. Functional analyses confirmed the upregulation of TGFβ/SMAD signaling and subsequently uncovered the involvement of two closely related transcription cofactors important in fibrogenesis, Yes-associated protein (YAP) and transcriptional coactivator with PDZ-binding motif (TAZ). Knocking down of FAM20C confirmed the TGFβ-YAP/TAZ interplay indicating that a profibrotic loop enabled gingival fibrosis in RNS patients. In summary, our in vivo and in vitro data provide a detailed description of the RNS gingival phenotype. They show that gingival fibrosis and calcifications are associated with, and most likely caused by excessed ECM production and disorganization. They furthermore uncover the contribution of increased TGFβ–YAP/TAZ signaling in the pathogenesis of the gingival fibrosis.
Published: 2024
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2. Variability of the response of human vaginal Lactobacillus crispatus to 17β-estradiol

Author: Maximilien Clabaut, Amine M. Boukerb, Amine Ben Mlouka, Amandine Suet, Ali Tahrioui, Julien Verdon, Magalie Barreau, Olivier Maillot, Agathe Le Tirant, Madina Karsybayeva, Coralie Kremser, Gérard Redziniak, Cécile Duclairoir-Poc, Chantal Pichon, Julie Hardouin, Pascal Cosette, Sylvie Chevalier, and Marc G. J. Feuilloley
Subjects: Medicine, Science
Abstract: Abstract We previously showed that the physiological concentration of 17β-estradiol in the vaginal environment is sufficient to affect the membrane dynamics and adhesion phenotype of the Lactobacillus crispatus strain CIP104459. However, L. crispatus is a heterogeneous species. Here, we investigated the effect of 17β-estradiol on the recently isolated L. crispatus vaginal strain V4, related to a cluster distant from CIP104459 and at the limit of being a different subspecies. Grown in the same medium, the two strains expressed a highly similar pool of proteins. However, in contrast to CIP104459, L. crispatus V4 showed high aggregation potential and 17β-estradiol promoted this phenotype. This effect was associated with large changes in cell-surface polarity and Lewis acid/base properties. In addition, we observed no effect on the membrane dynamics, contrary to CIP104459. These results can be explained by differences in the properties and organization of the S layer between the two strains. However, as for CIP104459, 17β-estradiol increased biosurfactant production of L. crispatus V4 and their adhesion to vaginal cells. This suggests that 17β-estradiol agonists would be valuable tools to favor a stable re-implantation of L. crispatus in the vaginal mucosa.
Published: 2021
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3. Proteomic and transcriptomic study of brain microvessels in neonatal and adult mice.

Author: Baptiste Porte, Clémence Chatelain, Julie Hardouin, Céline Derambure, Yasmine Zerdoumi, Michèle Hauchecorne, Nicolas Dupré, Soumeya Bekri, Bruno Gonzalez, Stéphane Marret, Pascal Cosette, and Philippe Leroux
Subjects: Medicine, Science
Abstract: Infants born before 29 weeks gestation incur a major risk of preterm encephalopathy and subependymal/intracerebral/intraventricular haemorrhage. In mice, an ontogenic window of haemorrhage risk was recorded up to 5 days after birth in serpine1 knock-out animals. Using proteome and transcriptome approaches in mouse forebrain microvessels, we previously described the remodelling of extracellular matrix and integrins likely strengthening the vascular wall between postnatal day 5 (P5) and P10. Haemorrhage is the ultimate outcome of vessel damage (i.e., during ischaemia), although discreet vessel insults may be involved in the aetiology of preterm encephalopathy. In this study, we examined proteins identified by mass spectrometry and segregating in gene ontology pathways in forebrain microvessels in P5, P10, and adult wild type mice. In parallel, comparative transcript levels were obtained using RNA hybridization microarrays and enriched biological pathways were extracted from genes exhibiting at least a two-fold change in expression. Five major biological functions were observed in those genes detected both as proteins and mRNA expression undergoing at least a two-fold change in expression in one or more age comparisons: energy metabolism, protein metabolism, antioxidant function, ion exchanges, and transport. Adult microvessels exhibited the highest protein and mRNA expression levels for a majority of genes. Energy metabolism-enriched gene ontology pathways pointed to the preferential occurrence of glycolysis in P5 microvessels cells versus P10 and adult preparations enriched in aerobic oxidative enzymes. Age-dependent levels of RNA coding transport proteins at the plasma membrane and mitochondria strengthened our findings based on protein data. The data suggest that immature microvessels have fewer energy supply alternatives to glycolysis than mature structures. In the context of high energy demand, this constraint might account for vascular damage and maintenance of the high bleeding occurrence in specific areas in immature brain.
Published: 2017
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4. Foxg1-Cre Mediated Lrp2 Inactivation in the Developing Mouse Neural Retina, Ciliary and Retinal Pigment Epithelia Models Congenital High Myopia.

Author: Olivier Cases, Antoine Joseph, Antoine Obry, Mathieu D Santin, Sirine Ben-Yacoub, Michel Pâques, Sabine Amsellem-Levera, Ana Bribian, Manuel Simonutti, Sébastien Augustin, Thomas Debeir, José Alain Sahel, Annabel Christ, Fernando de Castro, Stéphane Lehéricy, Pascal Cosette, and Renata Kozyraki
Subjects: Medicine, Science
Abstract: Myopia is a common ocular disorder generally due to increased axial length of the eye-globe. Its extreme form high myopia (HM) is a multifactorial disease leading to retinal and scleral damage, visual impairment or loss and is an important health issue. Mutations in the endocytic receptor LRP2 gene result in Donnai-Barrow (DBS) and Stickler syndromes, both characterized by HM. To clearly establish the link between Lrp2 and congenital HM we inactivated Lrp2 in the mouse forebrain including the neural retina and the retinal and ciliary pigment epithelia. High resolution in vivo MRI imaging and ophthalmological analyses showed that the adult Lrp2-deficient eyes were 40% longer than the control ones mainly due to an excessive elongation of the vitreal chamber. They had an apparently normal intraocular pressure and developed chorioretinal atrophy and posterior scleral staphyloma features reminiscent of human myopic retinopathy. Immunomorphological and ultrastructural analyses showed that increased eye lengthening was first observed by post-natal day 5 (P5) and that it was accompanied by a rapid decrease of the bipolar, photoreceptor and retinal ganglion cells, and eventually the optic nerve axons. It was followed by scleral thinning and collagen fiber disorganization, essentially in the posterior pole. We conclude that the function of LRP2 in the ocular tissues is necessary for normal eye growth and that the Lrp2-deficient eyes provide a unique tool to further study human HM.
Published: 2015
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5. Escherichia coli response to uranyl exposure at low pH and associated protein regulations.

Author: Arbia Khemiri, Marie Carrière, Nicolas Bremond, Mohamed Amine Ben Mlouka, Laurent Coquet, Isabelle Llorens, Virginie Chapon, Thierry Jouenne, Pascal Cosette, and Catherine Berthomieu
Subjects: Medicine, Science
Abstract: Better understanding of uranyl toxicity in bacteria is necessary to optimize strains for bioremediation purposes or for using bacteria as biodetectors for bioavailable uranyl. In this study, after different steps of optimization, Escherichia coli cells were exposed to uranyl at low pH to minimize uranyl precipitation and to increase its bioavailability. Bacteria were adapted to mid acidic pH before exposure to 50 or 80 µM uranyl acetate for two hours at pH≈3. To evaluate the impact of uranium, growth in these conditions were compared and the same rates of cells survival were observed in control and uranyl exposed cultures. Additionally, this impact was analyzed by two-dimensional differential gel electrophoresis proteomics to discover protein actors specifically present or accumulated in contact with uranium.Exposure to uranium resulted in differential accumulation of proteins associated with oxidative stress and in the accumulation of the NADH/quinone oxidoreductase WrbA. This FMN dependent protein performs obligate two-electron reduction of quinones, and may be involved in cells response to oxidative stress. Interestingly, this WrbA protein presents similarities with the chromate reductase from E. coli, which was shown to reduce uranyl in vitro.
Published: 2014
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6. Identification of S100A9 as biomarker of responsiveness to the methotrexate/etanercept combination in rheumatoid arthritis using a proteomic approach.

Author: Antoine Obry, Thierry Lequerré, Julie Hardouin, Olivier Boyer, Patrice Fardellone, Peggy Philippe, Xavier Le Loët, Pascal Cosette, and Olivier Vittecoq
Subjects: Medicine, Science
Abstract: One way to optimize the drug prescription in rheumatoid arthritis (RA) is to identify predictive biomarkers of drug responsiveness. Here, we investigated the potential "theranostic" value of proteins of the S100 family by monitoring levels of both S100A8 and S100A9 in blood samples from RA patients.For proteomic analysis, peripheral blood mononuclear cells (PBMC) and serum samples were collected in patients prior to initiation of the methotrexate/etanercept (MTX/ETA) combination. Firstly, relative mass spectrometry (MS) quantification focusing on S100A8 and S100A9 proteins was carried out from PBMCs samples to identify potential biomarkers. The same approach was also performed from serum samples from responder (R) and non responder (NR) patients. Finally, to confirm these results, an absolute quantification of S100A8, S100A9 proteins and calprotectin (heterodimer of S100A8/S100A9) was carried out on the serum samples using ELISA.MS analyses revealed that both S100A8 and S100A9 proteins were significantly accumulated in PBMC from responders. In contrast to PBMC, only the S100A9 protein was significantly overexpressed in the serum of R patients. Absolute quantification by ELISA confirmed this result and pointed out a similar expression level of S100A8 protein and calprotectin in sera from both R and NR groups. Thus, the S100A9 protein revealed to be predictive of MTX/ETA responsiveness, contrarily to parameters of inflammation and auto-antibodies which did not allow significant discrimination.This is the first report of an overexpression of S100A9 protein in both PBMCs and serum of patients with subsequent response to the MTX/ETA combination. This protein thus represents an interesting biomarker candidate of therapeutic response in RA.
Published: 2014
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7. Identification of biofilm-associated cluster (bac) in Pseudomonas aeruginosa involved in biofilm formation and virulence.

Author: Camille Macé, Damien Seyer, Chanez Chemani, Pascal Cosette, Patrick Di-Martino, Benoit Guery, Alain Filloux, Marc Fontaine, Virginie Molle, Guy-Alain Junter, and Thierry Jouenne
Subjects: Medicine, Science
Abstract: Biofilms are prevalent in diseases caused by Pseudomonas aeruginosa, an opportunistic and nosocomial pathogen. By a proteomic approach, we previously identified a hypothetical protein of P. aeruginosa (coded by the gene pA3731) that was accumulated by biofilm cells. We report here that a Delta pA3731 mutant is highly biofilm-defective as compared with the wild-type strain. Using a mouse model of lung infection, we show that the mutation also induces a defect in bacterial growth during the acute phase of infection and an attenuation of the virulence. The pA3731 gene is found to control positively the ability to swarm and to produce extracellular rhamnolipids, and belongs to a cluster of 4 genes (pA3729-pA3732) not previously described in P. aeruginosa. Though the protein PA3731 has a predicted secondary structure similar to that of the Phage Shock Protein, some obvious differences are observed compared to already described psp systems, e.g., this unknown cluster is monocistronic and no homology is found between the other proteins constituting this locus and psp proteins. As E. coli PspA, the amount of the protein PA3731 is enlarged by an osmotic shock, however, not affected by a heat shock. We consequently named this locus bac for biofilm-associated cluster.
Published: 2008
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8. Variability of the response of human vaginal Lactobacillus crispatus to 17β-estradiol

Author: Sylvie Chevalier, Maximilien Clabaut, Magalie Barreau, Gérard Redziniak, Madina Karsybayeva, Marc G. J. Feuilloley, Julie Hardouin, Agathe Le Tirant, Amine M. Boukerb, Cécile Duclairoir-Poc, Olivier Maillot, Amandine Suet, Amine Ben Mlouka, Julien Verdon, Pascal Cosette, Chantal Pichon, Coralie Kremser, Ali Tahrioui, Ecologie et biologie des interactions (EBI), Université de Poitiers-Centre National de la Recherche Scientifique (CNRS), Microbiologie de l'Eau (MDE), and Université de Poitiers-Centre National de la Recherche Scientifique (CNRS)-Université de Poitiers-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Physiology, Science, [SDV]Life Sciences [q-bio], 030106 microbiology, Microbiology, Article, 03 medical and health sciences, Membrane dynamics, Humans, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Lactobacillus crispatus, Multidisciplinary, Strain (chemistry), biology, Estradiol, Chemistry, Vaginal mucosa, Adhesion, biology.organism_classification, Phenotype, 030104 developmental biology, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Vagina, Medicine, Female, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, S-layer
Abstract: We previously showed that the physiological concentration of 17β-estradiol in the vaginal environment is sufficient to affect the membrane dynamics and adhesion phenotype of the Lactobacillus crispatus strain CIP104459. However, L. crispatus is a heterogeneous species. Here, we investigated the effect of 17β-estradiol on the recently isolated L. crispatus vaginal strain V4, related to a cluster distant from CIP104459 and at the limit of being a different subspecies. Grown in the same medium, the two strains expressed a highly similar pool of proteins. However, in contrast to CIP104459, L. crispatus V4 showed high aggregation potential and 17β-estradiol promoted this phenotype. This effect was associated with large changes in cell-surface polarity and Lewis acid/base properties. In addition, we observed no effect on the membrane dynamics, contrary to CIP104459. These results can be explained by differences in the properties and organization of the S layer between the two strains. However, as for CIP104459, 17β-estradiol increased biosurfactant production of L. crispatus V4 and their adhesion to vaginal cells. This suggests that 17β-estradiol agonists would be valuable tools to favor a stable re-implantation of L. crispatus in the vaginal mucosa.
Published: 2021
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9. LasB and CbpD Virulence Factors of Pseudomonas aeruginosa Carry Multiple Post-Translational Modifications on Their Lysine Residues

Author: Pascal Cosette, Charlotte Gaviard, Julie Hardouin, Thierry Jouenne, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-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)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)
Subjects: Virulence Factors, Lysine, Virulence, Human pathogen, Biology, medicine.disease_cause, Biochemistry, Microbiology, 03 medical and health sciences, Succinylation, Bacterial Proteins, medicine, [CHIM]Chemical Sciences, Humans, Electrophoresis, Gel, Two-Dimensional, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Pseudomonas aeruginosa, 030302 biochemistry & molecular biology, Metalloendopeptidases, General Chemistry, Lysine residue, 3. Good health, Acetylation, Posttranslational modification, [CHIM.OTHE]Chemical Sciences/Other, Carrier Proteins, Protein Processing, Post-Translational
Abstract: Pseudomonas aeruginosa is a multi-drug resistant human pathogen largely involved in nosocomial infections. Today, effective antibacterial agents are lacking. Exploring the bacterial physiology at the post-translational modifications (PTM) level may contribute to the renewal of fighting strategies. Indeed, some correlations between PTMs and the bacterial virulence, adaptation, and resistance have been shown. In a previous study performed in P. aeruginosa, we reported that many virulence factors like chitin-binding protein CbpD and elastase LasB were multiphosphorylated. Besides phosphorylation, other PTMs, like those occurring on lysine, seem to play key roles in bacteria. In the present study, we investigated for the first time the lysine succinylome and acetylome of the extracellular compartment of P. aeruginosa by using a two-dimensional immunoaffinity approach. Some virulence factors were identified as multimodified on lysine residues, among them, LasB and CbpD. Lysine can be modified by a wide range of chemical groups. In order to check the presence of other chemical groups on modified lysines identified on LasB and CbpD, we used 1- and 2- dimensional gel electrophoresis approaches to target lysine modified by 7 other modifications: butyrylation, crotonylation, dimethylation, malonylation, methylation, propionylation, and trimethylation. We showed that some lysines of these two virulence factors were modified by these 9 different PTMs. Interestingly, we found that the PTMs recovered on these two virulence factors were different than those previously reported in the intracellular compartment.
Published: 2019
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10. Antioxidant, antityrosinase and antibiofilm activities of synthesized peptides derived from Vicia faba protein hydrolysate: A powerful agents in cosmetic application

Author: Ines Karkouch, Mohamed Amine Ben Mlouka, Pascal Cosette, Ferid Limam, Christophe Rihouey, Salem Elkahoui, Dorra Gharbi, Laurent Coquet, Thierry Jouenne, Olfa Tabbene, Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-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)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, 2. Zero hunger, chemistry.chemical_classification, DPPH, [SDV]Life Sciences [q-bio], Tyrosinase, Peptide, 04 agricultural and veterinary sciences, Tandem mass spectrometry, Trypsin, 040401 food science, Hydrolysate, Vicia faba, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, 0404 agricultural biotechnology, chemistry, Biochemistry, Vicilin, medicine, Agronomy and Crop Science, ComputingMilieux_MISCELLANEOUS, medicine.drug
Abstract: The aim of this study was to identify peptides with antioxidant, antityrosinase and antibiofilm activities released from Vicia faba seed proteins hydrolysate. The hydrolysis pattern was performed with trypsin. Firstly, the obtained hydrolysate was fractionated by cation exchange chromatography and the fraction exhibiting the highest biological activity was then analyzed by reverse phase HPLC tandem mass spectrometry. After annotation by Peaks software (BSI, Canada) for de novo peptide sequencing, seven peptides were identified, mainly derived from storage proteins: legumin and vicilin. These peptides were further chemically synthesized to assess their antioxidant capacity, antityrosinase activity and antibiofilm ability against Pseudomonas aeruginosa PA14. Results showed that peptides P5, P6 and P7 identified as LSPGDVLVIPAGYPVAIK, VESEAGLTETWNPNHPELR and EEYDEEKEQGEEEIR respectively, displayed the highest DPPH radical scavenging activity (IC 50 = 0.25–1.9 mM). P5 was the only peptide able to chelate iron and reduce Fe 3+ to Fe 2+ . Furthermore, peptides P4 (GPLVHPQSQSQSN) and P6 were observed as potent tyrosinase inhibitors with IC 50 values of 1 and 0.14 mM respectively. P1, P5, P6 and P7 also showed interesting antibiofilm activity against Pseudomonas aeruginosa PA14 with MBIC 50 value ranged from 12 to 35 μM. Our data suggest that V. faba seed proteins hydrolysate could be potentially used as a source of natural bioactive peptides for cosmetic and pharmaceutical applications.
Published: 2017
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11. Neuroprotective effect of grape seed extract on brain ischemia: a proteomic approach

Author: Salem Elkhaoui, Sami Zekri, Ferid Limam, Mohamed El Ayed, Meherzia Mokni, Pascal Cosette, Safwen Kadri, Ezzedine Aouani, Thierry Jouenne, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine de Tunis, Université de Tunis El Manar (UTM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Faculté des Sciences de Bizerte [Université de Carthage], and Université de Carthage - University of Carthage
Subjects: Male, Proteomics, 0301 basic medicine, food.ingredient, Ischemia, Down-Regulation, Hippocampal formation, Biology, Pharmacology, medicine.disease_cause, Biochemistry, Neuroprotection, Antioxidants, Brain Ischemia, Rats, Sprague-Dawley, Brain ischemia, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, food, medicine, Animals, ComputingMilieux_MISCELLANEOUS, Grape Seed Extract, Dentate gyrus, Brain, medicine.disease, 3. Good health, Oxidative Stress, Neuroprotective Agents, 030104 developmental biology, Reperfusion Injury, Grape seed extract, Proteome, Neurology (clinical), [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress
Abstract: Stroke is one of the leading causes of long-lasting disability in human and oxidative stress an important underlying cause. Molecular insights into pathophysiology of ischemic stroke are still obscure, and the present study investigated the protective effect of high dosage Grape Seed Extract (GSE 2.5 g/kg) on brain ischemia-reperfusion (I/R) injury using a proteomic approach. Ischemia was realized by occlusion of the common carotid arteries for 30 min followed by 1 h reperfusion on control or GSE pre-treated rats, and a label-free quantification followed by mass spectrometry analysis used to evaluate I/R induced alterations in protein abundance and metabolic pathways as well as the protection afforded by GSE. I/R-induced whole brain ionogram dyshomeostasis, ultrastructural alterations, as well as inflammation into hippocampal dentate gyrus area, which were evaluated using ICP-OES, transmission electron microscopy and immuno-histochemistry respectively. I/R altered the whole brain proteome abundance among which 108 proteins were significantly modified (35 up and 73 down-regulated proteins). Eighty-four proteins were protected upon GSE treatment among which 27 were up and 57 down-regulated proteins, suggesting a potent protective effect of GSE close to 78%of the disturbed proteome. Furthermore, GSE efficiently prevented the brain from I/R-induced ion dyshomeostasis, ultrastructural alterations, inflammatory biomarkers as CD56 or CD68 and calcium burst within the hippocampus. To conclude, a potent protective effect of GSE on brain ischemia is evidenced and clinical trials using high dosage GSE should be envisaged on people at high risk for stroke.
Published: 2019
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12. Predictors of treatment response in rheumatoid arthritis

Author: Pascal Cosette, Céline Derambure, Olivier Vittecoq, Thierry Lequerré, Pascal Rottenberg, CHU Bois-Guillaume, UNIROUEN - UFR Santé (UNIROUEN UFR Santé), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Génomique et Médecine Personnalisée du Cancer et des Maladies Neuropsychiatriques (GPMCND), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de rhumatologie [CHU Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and CCSD, Accord Elsevier
Subjects: Drug, Male, medicine.medical_specialty, Treatment response, [SDV.IMM] Life Sciences [q-bio]/Immunology, Proteome, media_common.quotation_subject, Risk Assessment, Severity of Illness Index, Arthritis, Rheumatoid, 03 medical and health sciences, 0302 clinical medicine, Rheumatology, Predictive Value of Tests, Rheumatoid Factor, Response prediction, medicine, Rheumatoid factor, Humans, 030212 general & internal medicine, Precision Medicine, Rheumatoid arthritis, Intensive care medicine, media_common, 030203 arthritis & rheumatology, [SDV.MHEP.RSOA] Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal system, Biological Products, business.industry, medicine.disease, Prognosis, Theranostics, 3. Good health, Review article, Clinical Practice, Treatment Outcome, [SDV.MHEP.RSOA]Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal system, Antirheumatic Agents, [SDV.IMM]Life Sciences [q-bio]/Immunology, Identification (biology), Drug Therapy, Combination, Female, Personalized medicine, Patient Safety, business, Transcriptome, Biomarkers
Abstract: International audience; The expanding array of drugs available for treating rheumatoid arthritis is creating challenges in drug selection for the individual patient. The identification of biomarkers that predict the treatment response prior to drug exposure is therefore a current priority. This new approach, known as theranostics, is a component of personalized medicine, which involves selecting the management strategies that are most effective for a given patient at a given point in time. Antibodies to citrullinated peptides, rheumatoid factor, and the interferon signature are the most robust and best validated biomarkers identified to date. Matrices containing clinical or laboratory parameters of diagnostic or prognostic relevance may help to select the best treatment for the individual patient. Furthermore, the development of large-scale approaches requiring no a priori knowledge, such as functional genomics and metabolomics, hold considerable promise, despite persistent difficulties in replicating findings. The complexity of the treatment response in a given patient and substantial variability across patients suggest that biomarkers may be more helpful in combination than singly. The objectives of this review article are to discuss the approaches used to identify theranostic biomarkers and to present an overview of currently available biomarkers and of their performance in everyday clinical practice. However, the range of biomarkers suitable for use in daily practice remains extremely narrow.
Published: 2019
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13. Lysine Succinylation and Acetylation in Pseudomonas aeruginosa

Author: Charlotte Gaviard, Thierry Jouenne, Isabelle Broutin, Julie Hardouin, Emmanuelle Dé, Pascal Cosette, Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Polymères Biopolymères Surfaces (PBS), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Polymères, biopolymères, membranes (PBM), Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), and Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN)
Subjects: 0301 basic medicine, Proteomics, 030106 microbiology, Lysine, Succinic Acid, Virulence, medicine.disease_cause, Tandem mass spectrometry, Biochemistry, Citric Acid, 03 medical and health sciences, Succinylation, Bacterial Proteins, medicine, [CHIM]Chemical Sciences, ComputingMilieux_MISCELLANEOUS, biology, Pseudomonas aeruginosa, Chemistry, Acetylation, General Chemistry, biology.organism_classification, 3. Good health, 030104 developmental biology, bacteria, [CHIM.OTHE]Chemical Sciences/Other, Protein Processing, Post-Translational, Bacteria
Abstract: Pseudomonas aeruginosa is a multi-drug-resistant human opportunistic pathogen largely involved in nosocomial infections. Unfortunately, effective antibacterial agents are lacking. Exploring its physiology at the post-translational modifications (PTMs) level may contribute to the renewal of combat tactics. Recently, lysine succinylation was discovered in bacteria and seems to be an interesting PTM. We present the first succinylome and acetylome of P. aeruginosa PA14 cultured in the presence of four different carbon sources using a 2D immunoaffinity approach coupled to nanoliquid chromatography tandem mass spectrometry. A total of 1520 succinylated (612 proteins) and 1102 acetylated (522 proteins) lysine residues were characterized. Citrate was the carbon source in which we identified the higher number of modified proteins. Interestingly, 622 lysine residues (312 proteins) were observed either acetylated or succinylated. Some of these proteins, were involved in virulence, adaptation, resistance, and so on. A label-free quantification points out the existence of different protein forms for a same protein (unmodified, succinylated or acetylated) and suggests different abundance as a function of the carbon sources. This work is a promising starting point for further investigations on the biological role of lysine succinylation in P. aeruginosa.
Published: 2018
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14. Proteomic profiling of lysine acetylation in Pseudomonas aeruginosa reveals the diversity of acetylated proteins

Author: Thierry Jouenne, Tassadit Ouidir, Pascal Cosette, and Julie Hardouin
Subjects: chemistry.chemical_classification, 0303 health sciences, 030306 microbiology, Proteomic Profiling, Pseudomonas aeruginosa, Lysine, Biology, medicine.disease_cause, Proteomics, Biochemistry, 03 medical and health sciences, Metabolic pathway, chemistry.chemical_compound, Enzyme, chemistry, Biosynthesis, Acetylation, medicine, Molecular Biology, 030304 developmental biology
Abstract: Protein lysine acetylation is a reversible and highly regulated post-translational modification with the well demonstrated physiological relevance in eukaryotes. Recently, its important role in the regulation of metabolic processes in bacteria was highlighted. Here, we reported the lysine acetylproteome of Pseudomonas aeruginosa using a proteomic approach. We identified 430 unique peptides corresponding to 320 acetylated proteins. In addition to the proteins involved in various metabolic pathways, several enzymes contributing to the lipopolysaccharides biosynthesis were characterized as acetylated. This data set illustrated the abundance and the diversity of acetylated lysine proteins in P. aeruginosa and opens opportunities to explore the role of the acetylation in the bacterial physiology.
Published: 2015
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15. Brain proteomic modifications associated to protective effect of grape extract in a murine model of obesity

Author: Safwen Kadri, Ferid Limam, Selima Smine, Pascal Cosette, Thierry Jouenne, Manuel Fréret, Julie Hardouin, Ezzedine Aouani, Mohamed Amri, Antoine Obry, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Faculté des Sciences Mathématiques, Physiques et Naturelles de Tunis (FST), Université de Tunis El Manar (UTM), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Faculté des Sciences de Bizerte [Université de Carthage], Université de Carthage - University of Carthage, Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: 0301 basic medicine, Proteomics, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Biophysics, Pharmacology, Biology, medicine.disease_cause, Diet, High-Fat, Biochemistry, Antioxidants, Mass Spectrometry, Analytical Chemistry, 03 medical and health sciences, Mice, 0302 clinical medicine, Pharmacotherapy, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Animals, Humans, Glycolysis, Calcium Signaling, Obesity, Molecular Biology, Calcium signaling, Grape Seed Extract, Brain, food and beverages, medicine.disease, 3. Good health, Rats, Oxidative Stress, 030104 developmental biology, Lipotoxicity, Gene Expression Regulation, Murine model, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress
Abstract: International audience; n recent years, the obesity epidemic has developed into a major health crisis worldwide. With current treatments limited to expensive, high-risk surgery and minimally efficacious pharmacotherapy, new therapeutic options are urgently needed to fight against this alarming trend. Though brain dysfunction has been studied linked to high fat diet (HFD) and grape seed and skin extract (GSSE) correction, the proteomic modifications linking the two effects on brain lipotoxicity are not well understood. To this end rats were exposed for 8 weeks to HFD treatment, to GSSE (500 mg/kg BW) and to binary mixture of HFD and GSSE to gain insight into the potential pathways altered with metabolic disease and the protection afforded by GSSE. Significant modifications of brain proteins were detected using mass spectrometry-based differential proteomics. These proteins were mainly related to oxidative stress, glycolysis and calcium signaling. Additionally, proteins involved in the cytoskeleton were also affected by HFD treatment. Interestingly, whether up- or down regulated protein abundances, GSSE corrected most of the disturbances of HFD treatment. These findings provide impetus for future therapeutic investigation on GSSE against other metabolic disorders.
Published: 2017
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16. Neuroprotective Activity of Grape Seed and Skin Extract Against Lithium Exposure Using Proteomic Research

Author: Olfa Khazri, Ferid Limam, Pascal Cosette, Abdelhafidh Khazri, Ezzeddine Aouani, Ali Mezni, Faculté des Sciences de Bizerte [Université de Carthage], Université de Carthage - University of Carthage, Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: 0301 basic medicine, Male, Proteomics, food.ingredient, Proteome, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Neuroscience (miscellaneous), Lithium, medicine.disease_cause, Neuroprotection, 03 medical and health sciences, Cellular and Molecular Neuroscience, 0302 clinical medicine, food, Phenols, Tandem Mass Spectrometry, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], medicine, Animals, Protein Interaction Maps, Rats, Wistar, Grape Seed Extract, Proteomic research, Chemistry, Brain, Wistar rats, Oxidative Stress, 030104 developmental biology, Neuroprotective Agents, Neurology, Biochemistry, GSSE, Grape seed extract, Phosphoprotein, Toxicity, Signal transduction, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, 030217 neurology & neurosurgery, Oxidative stress, Chromatography, Liquid
Abstract: International audience; Lithium (Li) has raised scientific concern because it represents a serious problem threatening human health. This study aimed firstly at analyzing and potentially quantifying the impact of Li and grape seed and skin extract (GSSE) separately and, secondly, describing the possible neuroprotective activity of GSSE against Li toxicity. To this end, rats were exposed for 30 days to different Li concentrations (0, 2, and 100 mg/kg bw), to GSSE (4000 mg/kg bw), and to binary mixture of Li and GSSE. Liquid chromatography (HPLC–MS/MS) analysis used for GSSE showed that 15 phenolic compounds are present in the extract. Significant modifications of proteins were detected in the brain using proteomics research after treatment. Proteins were successfully identified by a linear ion trap–Orbitrap mass spectrometer. These proteins can be roughly related to oxidative stress, glycolysis, signaling pathway, and inflammation. Additionally, proteins involved in cell junction such as myosin, spectrin, tubulin, ERM-binding phosphoprotein, and dynein were also affected by Li exposure. Dose response was detected for most expressed proteins after Li treatment. In contrast, GSSE induced the expression and/or the stabilization of some proteins changed after Li treatment in the brain showing its neuroprotective activity. These data demonstrate that proteomic analysis is a powerful tool to provide valuable insights into mechanisms of toxicity of Li in the nervous system of Wistar rats. To our knowledge, this is the first evidence of using GSSE as neuroprotective model against Li toxicity. These findings provide impetus for future investigation on GSSE against other toxic chemicals.
Published: 2017
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17. Impaired vitreous composition and retinal pigment epithelium function in the FoxG1::LRP2 myopic mice

Author: Pascal Cosette, Sébastien Augustin, Sirine Ben-Yacoub, Antoine Obry, Manuel Simonutti, Géraldine Toutirais, Renata Kozyraki, Olivier Cases, Antoine Joseph, Annabel Christ, HAL-UPMC, Gestionnaire, Institut de la Vision, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Microscopie Electronique [IBPS] (IBPS-ME), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Max Delbrück Center for Molecular Medicine [Berlin] (MDC), Helmholtz-Gemeinschaft = Helmholtz Association, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Polymères Biopolymères Surfaces (PBS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC), Acides nucléiques : dynamique, ciblage, et fonctions biologiques - Régulation et dynamique des génomes (ANDCFB), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Max Delbrück Center for Molecular Medicine [Berlin], and Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN)
Subjects: 0301 basic medicine, genetic structures, Endocytic cycle, Mice, Transgenic, Nerve Tissue Proteins, Retinal Pigment Epithelium, Biology, Vitreous, Pathogenesis, Mice, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, low density lipoprotein receptor-related protein 2, lipoprotein receptor-related protein 2, High myopia, Myopia, medicine, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organs, Molecular Biology, Retinal pigment epithelium, ADP-Ribosylation Factors, Retinal detachment, Forkhead Transcription Factors, Anatomy, medicine.disease, LRP2, eye diseases, Endocytosis, Cell biology, Vitreous Body, Low Density Lipoprotein Receptor-Related Protein-2, 030104 developmental biology, medicine.anatomical_structure, chemistry, [SDV.MHEP.OS] Life Sciences [q-bio]/Human health and pathology/Sensory Organs, Low-density lipoprotein, 030221 ophthalmology & optometry, Molecular Medicine, low density, sense organs, Homeostasis, Retinopathy
Abstract: International audience; High myopia (HM) is one of the main causes of visual impairment and blindness all over the world and an unsolved medical problem. Persons with HM are predisposed to other eye pathologies such as retinal detachment, myopic retinopathy or glaucomatous optic neuropathy, complications that may at least partly result from the extensive liquefaction of the myopic vitreous gel. To identify the involvement of the liquid vitreous in the pathogenesis of HM we here analyzed the vitreous of the recently described highly myopic low density lipoprotein receptor-related protein 2 (Lrp2)-deficient eyes. Whereas the gel-like fraction was not apparently modified, the volume of the liquid vitreous fraction (LVF) was much higher in the myopic eyes. Biochemical and proteome analysis of the LVF revealed several modifications including a marked decrease of potassium, sodium and chloride, of proteins involved in ocular tissue homeostasis and repair as well as of ADP-ribosylation factor 4 (ARF4), a protein possibly involved in LRP2 trafficking. A small number of proteins, mainly comprising known LRP2 ligands or proteins of the inflammatory response, were over expressed in the mutants. Moreover the morphology of the LRP2-deficient retinal pigment epithelium (RPE) cells was affected and the expression of ARF4 as well as of proteins involved in degradative endocytosis was strongly reduced. Our results support the idea that impairment of the RPE structure and most likely endocytic function may contribute to the vitreal modifications and pathogenesis of HM.
Published: 2017
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18. The aliphatic amidase AmiE is involved in regulation of Pseudomonas aeruginosa virulence

Author: Pascal Cosette, Alain Dufour, Alexandre Crépin, Sylvie Chevalier, Pierre Cornelis, Julie Hardouin, Thibaut Rosay, Julien Vieillard, Perrine Bortolotti, Thomas Clamens, Joerg Overhage, Benoit Guery, Fergal O'Gara, Takfarinas Kentache, Anke Neidig, Teddy Grandjean, Marc G. J. Feuilloley, Marlies J. Mooij, Emeline Bouffartigues, Mélanie Hillion, Olivier Lesouhaitier, Laboratoire de Microbiologie Signaux et Microenvironnement (LMSM), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de Biotechnologie et Chimie Marines (LBCM), Université de Brest (UBO)-Université de Bretagne Sud (UBS)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS), Recherche translationelle relations hôte-pathogènes, Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Université Lille 2 - Faculté de Médecine, Karlsruhe Institute of Technology (KIT), University College Cork (UCC), Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Biologie et physiologie des états septiques, IFR114-Université de Lille, Droit et Santé, This work was supported by grants from the Communauté d’Agglomération d’Evreux, the Conseil Général de l′Eure, European Union (FEDER), the French Association 'Vaincre la Mucoviscidose' and the Partenariats Hubert Curien (PHC Ulysses). Financial support by the BioInterfaces (BIF) Program of the Karlsruhe Institute of Technology (KIT) in the Helmholtz Association is gratefully acknowledged., We wish to thank Magalie Barreau and Olivier Maillot for technical assistance. T. Clamens and T. Rosay are recipients of a doctoral fellowship from the French Ministry of Research (MRE)., Vriendenkring VUB, Microbiology, Université de Bretagne Sud (UBS)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), 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)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine Henri Warembourg - Université de Lille, Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-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)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-High-tech Research Infrastructures for Life Sciences (HeRacLeS), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Bazire, Alexis
Subjects: Male, 0301 basic medicine, Virulence regulation, MESH: Pseudomonas Infections/microbiology, Proteome, health care facilities, manpower, and services, MESH: Dictyostelium/microbiology, MESH: Virulence, medicine.disease_cause, MESH: Quorum Sensing, Pilus, chemistry.chemical_compound, MESH: Caenorhabditis elegans/microbiology, MESH: Amidohydrolases/metabolism, AmiE overproduction, Dictyostelium, MESH: Animals, Lung, health care economics and organizations, MESH: Pseudomonas aeruginosa/enzymology, Multidisciplinary, Virulence, Quorum Sensing, MESH: Proteome, Pseudomonas aeruginosa, Female, Life sciences, biology, MESH: Virulence Factors, Virulence Factors, 030106 microbiology, Homoserine, MESH: Biofilms, Biology, Microbiology, Article, Amidohydrolases, Amidase, 03 medical and health sciences, Pyocyanin, MESH: Mice, Inbred C57BL, ddc:570, Journal Article, medicine, Animals, Pseudomonas Infections, cardiovascular diseases, Caenorhabditis elegans, MESH: Lung/microbiology, MESH: Pseudomonas aeruginosa/pathogenicity, Biofilm, Bacteriology, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Male, MESH: Pseudomonas Infections/enzymology, Mice, Inbred C57BL, Quorum sensing, chemistry, Biofilms, FOS: Biological sciences, Pseudomonas aeruginosa virulence, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Female
Abstract: We have previously shown that the eukaryotic C-type natriuretic peptide hormone (CNP) regulates Pseudomonas aeruginosa virulence and biofilm formation after binding on the AmiC sensor, triggering the amiE transcription. Herein, the involvement of the aliphatic amidase AmiE in P. aeruginosa virulence regulation has been investigated. The proteome analysis of an AmiE over-producing strain (AmiE+) revealed an expression change for 138 proteins, including some that are involved in motility, synthesis of quorum sensing compounds and virulence regulation. We observed that the AmiE+ strain produced less biofilm compared to the wild type, and over-produced rhamnolipids. In the same line, AmiE is involved in P. aeruginosa motilities (swarming and twitching) and production of the quorum sensing molecules N-acyl homoserine lactones and Pseudomonas Quinolone Signal (PQS). We observed that AmiE overproduction reduced levels of HCN and pyocyanin causing a decreased virulence in different hosts (i.e. Dictyostelium discoideum and Caenorhabditis elegans). This phenotype was further confirmed in a mouse model of acute lung infection, in which AmiE overproduction resulted in an almost fully virulence decrease. Taken together, our data suggest that, in addition to its role in bacterial secondary metabolism, AmiE is involved in P. aeruginosa virulence regulation by modulating pilus synthesis and cell-to-cell communication.
Published: 2017
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19. Major remodeling of brain microvessels during neonatal period in the mouse: A proteomic and transcriptomic study

Author: Antoine Obry, Baptiste Porte, Thierry Lequerré, Soumeya Bekri, Yasmine Zerdoumi, Bruno J. Gonzalez, Céline Derambure, Philippe Leroux, Julie Hardouin, Pascal Cosette, Nicolas Dupré, Jean-Michel Flaman, Michèle Hauchecorne, Stéphane Marret, Endothélium microcirculatoire cérébral et lésions du système nerveux central au cours du développement (Néovasc), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génomique et Médecine Personnalisée du Cancer et des Maladies Neuropsychiatriques (GPMCND), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Génétique du cancer et des maladies neuropsychiatriques (GMFC), Service de rhumatologie [CHU Rouen], CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Physiopathologie et biothérapies des maladies inflammatoires et autoimmunes, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de biochimie générale [Rouen], Normandie Université (NU)-Centre hospitalier universitaire de Rouen, Maladies neurodéveloppementales et neurovasculaires (NeuroDiderot (UMR_S_1141 / U1141)), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA), Team 4 'NeoVasc' - INSERM U1245, Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Service de rhumatologie [Rouen], Normandie Université (NU)-Normandie Université (NU)-CHU Rouen, Institut de Physique du Globe de Paris (IPGP), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut national des sciences de l'Univers (INSU - CNRS)-IPG PARIS-Université Paris Diderot - Paris 7 (UPD7)-Université de La Réunion (UR)-Centre National de la Recherche Scientifique (CNRS), Schulich School of Music & CIRMMT, and McGill University
Subjects: Male, Proteomics, 0301 basic medicine, Proteases, Proteome, Microarray, [SDV]Life Sciences [q-bio], Vascular Remodeling, Bioinformatics, Transcriptome, Andrology, Extracellular matrix, Mice, 03 medical and health sciences, 0302 clinical medicine, Subependymal zone, Animals, Medicine, ComputingMilieux_MISCELLANEOUS, Cerebral Hemorrhage, business.industry, Glutamate receptor, Brain, Gene Expression Regulation, Developmental, Original Articles, medicine.disease, Mice, Inbred C57BL, 030104 developmental biology, Intraventricular hemorrhage, Neurology, Microvessels, Forebrain, Female, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Neurology (clinical), Cardiology and Cardiovascular Medicine, business, 030217 neurology & neurosurgery
Abstract: Preterm infants born before 29 gestation weeks incur major risk of subependymal/intracerebral/intraventricular hemorrhage. In mice, neonate brain endothelial cells are more prone than adult cells to secrete proteases under glutamate challenge, and invalidation of the Serpine 1 gene is accompanied by high brain hemorrhage risk up to five days after birth. We hypothesized that the structural and functional states of microvessels might account for age-dependent vulnerability in mice up to five days after birth and might represent a pertinent paradigm to approach the hemorrhage risk window observed in extreme preterms. Mass spectrometry proteome analyses of forebrain microvessels at days 5, 10 and in adult mice revealed 899 proteins and 36 enriched pathways. Microarray transcriptomic study identified 5873 genes undergoing at least two-fold change between ages and 93 enriched pathways. Both approaches pointed towards extracellular matrix, cell adhesion and junction pathways, indicating delayed microvascular strengthening after P5. Furthermore, glutamate receptors, proteases and their inhibitors exhibited convergent evolutions towards excitatory aminoacid sensitivity and low proteolytic control likely accounting for vascular vulnerability in P5 mice. Thus, age vascular specificities must be considered in future therapeutic interventions in preterms. Data are available on ProteomeXchange (identifier PXD001718) and NCBI Gene-Expression-Omnibus repository (identification GSE67870).
Published: 2016
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20. Anti-Candida effect of bacillomycin D-like lipopeptides from Bacillus subtilis B38

Author: Abdelhamid Gharbi, Imen Ben Slimene, Thierry Jouenne, Maria Luisa Mangoni, Leila Kalai, Olfa Tabbene, Ines Karkouch, Salem Elkahoui, Pascal Cosette, and Ferid Limam
Subjects: 0303 health sciences, Bacillaceae, biology, 030306 microbiology, Lipopeptide, Bacillus subtilis, biology.organism_classification, medicine.disease, Microbiology, Bacillales, Corpus albicans, Hemolysis, 3. Good health, 03 medical and health sciences, chemistry.chemical_compound, Bacillomycin, chemistry, Genetics, medicine, Candida albicans, Molecular Biology, 030304 developmental biology
Abstract: Bacillus subtilis B38, isolated from soil, showed antimicrobial activity against human pathogenic Candida albicans species. Specific PCR primers revealed the presence of the bamC gene, which is involved in the biosynthesis of bacillomycin D. Three anti-Candida compounds designated a(1) , a(2) and a(3) were purified from culture supernatant and identified using matrix-assisted laser desorption/ionization time-of-flight MS as analogues of bacillomycin D-like lipopeptides of 14, 15 and 16 carbon fatty acid long chains, respectively. The compound a(3) displayed the strongest fungicidal activity against pathogenic C. albicans strains. It was even more active than amphotericin B with a lethal concentration of 59.07 vs. 135.26 μM of the antimycotic drug against the pathogenic strain C. albicans sp. 311 isolated from finger nail. Only moderate or weak anti-Candida activity was recorded for a(1) and a(2) compounds. Furthermore, a(3) showed the highest hemolytic activity, reaching 50% hemolysis at 22.14 μM, whereas a(1) and a(2) displayed a limited hemolysis at 68.26 and 37.41 μM, respectively. These findings suggest that the acyl chain length of bacillomycin D-like lipopeptides plays a major role in hemolytic and antifungal activities.
Published: 2011
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21. Peroxiredoxin 2 is Involved in the Neuroprotective Effects of PACAP in Cultured Cerebellar Granule Neurons

Author: Alain Fournier, Pascal Cosette, David Vaudry, Magalie Bénard, Béatrice Botia, Aurélia Ravni, Bruno J. Gonzalez, Anthony Falluel-Morel, Damien Seyer, Hubert Vaudry, Thierry Jouenne, Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-CHU Rouen, Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), International Associated laboratory Samuel de Champlain, Institut National de la Recherche Scientifique [Québec] (INRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Institut Armand Frappier (INRS-IAF), Institut National de la Recherche Scientifique [Québec] (INRS)-Réseau International des Instituts Pasteur (RIIP), and This work was supported by INSERM (U413), the European Institute for Peptide Research (IFRMP23), the Institut de Recherches Scientifiques sur les Boissons (IREB), an Interreg 3A FEDER project, the ANR (06-JCJC-0071), and the Conseil Régional de Haute-Normandie. The work was conducted with the technical support of the proteomic facility of the IFRMP23 and the Platform for Cell Imaging of Haute-Normandie. BB was a recipient of a doctoral fellowship from the Société Française d’Alcoologie and a fellowship from the Fondation pour la Recherche Médicale. We thank Dr Mickaël Naassila for the quantification of ethanol level in blood samples.
Subjects: Small interfering RNA, [SDV]Life Sciences [q-bio], MESH: RNA, Small Interfering/genetics, MESH: Cerebellum/cytology, MESH: Amino Acid Sequence, 0302 clinical medicine, Cerebellum, MESH: Animals, RNA, Small Interfering, Cells, Cultured, MESH: Neurons/cytology, Neurons, 0303 health sciences, biology, medicine.diagnostic_test, Caspase 3, MESH: Pituitary Adenylate Cyclase-Activating Polypeptide/metabolism, General Medicine, respiratory system, 3. Good health, Neuroprotective Agents, MESH: Colforsin/metabolism, Pituitary Adenylate Cyclase-Activating Polypeptide, Tetradecanoylphorbol Acetate, hormones, hormone substitutes, and hormone antagonists, MESH: Cells, Cultured, Neurotrophin, endocrine system, MESH: Rats, Molecular Sequence Data, MESH: Neuroprotective Agents/metabolism, Adenylate kinase, Peroxiredoxin 2, Neuroprotection, MESH: Peroxiredoxins/metabolism, MESH: Ethanol/metabolism, 03 medical and health sciences, Cellular and Molecular Neuroscience, Western blot, MESH: Peroxiredoxins/genetics, medicine, Animals, Amino Acid Sequence, Rats, Wistar, Protein kinase C, 030304 developmental biology, MESH: Molecular Sequence Data, Ethanol, Colforsin, MESH: Neurons/metabolism, Peroxiredoxins, MESH: Rats, Wistar, Molecular biology, Rats, MESH: Tetradecanoylphorbol Acetate/metabolism, MESH: RNA, Small Interfering/metabolism, biology.protein, MESH: Pituitary Adenylate Cyclase-Activating Polypeptide/genetics, MESH: Caspase 3/metabolism, 030217 neurology & neurosurgery
Abstract: International audience; The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) is known to counteract in vitro the deleterious effects of toxic agents on cerebellar granule cell survival and differentiation. The potent antiapoptotic action of PACAP is mediated through inhibition of caspase-3 activity; however, additional proteins are likely involved and remain to be identified. Two-dimensional gel electrophoresis analysis coupled with mass spectrometry characterization led to the identification of a protein, peroxiredoxin 2, which was induced after a 6-h treatment with PACAP. Western blot analysis confirmed the regulation of peroxiredoxin 2 by PACAP and revealed that this protein is induced by both cyclic AMP and protein kinase C stimulators. Inhibition of peroxiredoxin 2 expression, using two distinct small-interfering RNAs (siRNAs), reduced the effect of PACAP on caspase-3 activity and cerebellar granule cell survival. Peroxiredoxin 2 expression was also induced in vivo and in vitro by ethanol. Although ethanol and PACAP exert opposite effects on caspase-3 activity, inhibition of peroxiredoxin 2 expression, using siRNAs, only reduced the ability of PACAP to prevent ethanol-induced caspase-3 activity. Taken together, these data indicate that peroxiredoxin 2 is probably involved in the neurotrophic effect of PACAP and suggest that this protein may have a therapeutic potential for the treatment of some neurodegenerative diseases
Published: 2008
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22. Suspension-cultured BY-2 tobacco cells produce and mature immunologically active house dust mite allergens

Author: Caroline Bonneau, Pascal Cosette, Olivia Tran Dinh, Véronique Gomord, François Dorlhac de Borne, Erika van Oort, David Lienard, Philippe Moingeon, Muriel Bardor, Ronald van Ree, Loïc Faye, Alain Didierlaurent, Laurence Van Overtvelt, Eric Wambre, Rene Delon, AII - Amsterdam institute for Infection and Immunity, APH - Amsterdam Public Health, and Experimental Immunology
Subjects: Allergy, medicine.medical_treatment, Cell Culture Techniques, Plant Science, medicine.disease_cause, law.invention, Allergen, law, Tobacco, medicine, Animals, House dust mite, biology, Immunogenicity, Pyroglyphidae, Immunotherapy, Allergens, Plants, Genetically Modified, biology.organism_classification, medicine.disease, Recombinant Proteins, respiratory tract diseases, Immunology, Recombinant DNA, Agronomy and Crop Science, Biotechnology
Abstract: The replacement of crude allergen extracts by selected allergens currently represents a major goal for the improvement of allergy diagnosis and immunotherapy. Indeed, the development of molecularly defined vaccines would facilitate both standardization and enhance batch-to-batch reproducibility as well as treatment specificity. In this study, we have investigated the potential of tobacco plant cells to produce biologically active forms of the two major allergens from the house dust mite. A detailed characterization of these plant-made allergens has shown similar proteolytic maturation and folding as well as comparable immunoreactivity to their natural counterparts. Altogether, our results exemplify that suspension-cultured BY-2 tobacco cells represent a low cost and environmentally safe expression system suitable to produce recombinant allergens from Dermatophagoides pteronyssinus under a form appropriate for diagnostic and therapeutic purposes.
Published: 2007
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23. Characterization of new outer membrane proteins of Pseudomonas aeruginosa using a combinatorial peptide ligand library

Author: Emmanuelle Dé, Pascal Cosette, Thierry Jouenne, Julie Hardouin, Arbia Khemiri, Philippe Chan Tchi Song, Mohamed Amine Ben Mlouka, Damien Seyer, Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Two-dimensional gel electrophoresis, biology, Chemistry, Pseudomonas aeruginosa, [SDV]Life Sciences [q-bio], Albumin, Shotgun, biology.organism_classification, medicine.disease_cause, Biochemistry, Blood proteins, Molecular biology, Analytical Chemistry, Membrane protein, Peptide Library, medicine, Electrophoresis, Gel, Two-Dimensional, Bacterial outer membrane, Bacteria, ComputingMilieux_MISCELLANEOUS, Bacterial Outer Membrane Proteins
Abstract: Most often, the use of ProteoMiner beads has been restricted to human serum proteins for the normalization of major proteins, such as albumin. However, there are other situations of interest in which the presence of major proteins would quench the signals of low abundance polypeptides. We propose the use of these beads for investigating the envelope of the gram-negative bacterium Pseudomonas aeruginosa. Initially, we performed comparative 2D electrophoresis to qualitatively evaluate the incidence of the normalization stage. This demonstrated a significant reduction of the major membrane proteins. Thereafter, using shotgun analysis, the same protein extract was targeted by using combinatorial peptide ligand library capture. This treatment yielded 154 additional outer membrane proteins (OMPs) uncovered by the study of the crude sample.
Published: 2015
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24. Characterization of N-terminal protein modifications in Pseudomonas aeruginosa PA14

Author: Pascal Cosette, Julie Hardouin, Tassadit Ouidir, Frédérique Jarnier, Thierry Jouenne, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Proteomics, Proteome, Molecular Sequence Data, Amino-Acid N-Acetyltransferase, Biophysics, Peptide, Cleavage (embryo), medicine.disease_cause, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Methionine, Bacterial Proteins, medicine, [CHIM]Chemical Sciences, Amino Acid Sequence, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, Pseudomonas aeruginosa, 030302 biochemistry & molecular biology, Acetylation, biology.organism_classification, Bacterial Processes, Peptide Fragments, chemistry, Protein Processing, Post-Translational, Bacteria
Abstract: Even though protein initiator methionine excision (NME) and N-terminal acetylation (NTA) have been relatively well investigated in eukaryotic proteomes, few studies were dedicated to these modifications in bacteria up to now. In this work, we investigated, for the first time, the N-terminal proteome of the bacterium Pseudomonas aeruginosa PA14 by studying the NME and NTA processes using proteomic approaches. For NME, most of proteins had their initiator Met cleaved (63%) and the nature of the penultimate residue seems to be essential for this cleavage. Concerning NTA, two methods were applied (protein fractionation and peptide enrichment). This allowed us to identify 117 Nα-acetylated proteins, among them 113 have not yet been described as modified in bacteria. Most often, the non-acetylated form was over-represented compared to the acetylated form, arguing that this latter was a minor part of the total abundance of a given protein. Furthermore, some proteins with acetylated initiator methionine were observed. The present work significantly enlarges the number of N-terminally modified proteins in bacteria and confirms that these modifications are a general and fundamental process, not only restricted to eukaryotes. Biological significance Protein modifications in prokaryotes have been detected more recently than in eukaryotes. Methionine cleavage and N-terminal acetylation are two common protein N-terminal modifications. Despite their importance in bacterial processes, they are less investigated. The characterization of N-terminal acetylation in bacteria is a challenge because no antibody exists and it is a less frequent modification than in eukaryotes. We used proteomic approaches (enrichment, fractionation, nanoLC–MS/MS, and bioinformatic analyses) to investigate the N-terminal methionine excision and to profile the N-terminal acetylome of P. aeruginosa strain PA14. From our results, around 60% of the proteins had their iMet cleaved. In total, 117 proteins were identified constituting the largest dataset in prokaryotes. Among them, proteins kept their initiator methionine and were acetylated. These results may facilitate the design of experiments to better understand the role of acetylation at the protein N-terminus of P. aeruginosa PA14.
Published: 2015
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25. Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures

Author: Réal Lemieux, Muriel Bardor, Michèle Dargis, Sonia Trépanier, Catherine Lange, Thomas Paccalet, Pascal Cosette, Corinne Loutelier-Bourhis, Anne-Catherine Fitchette, Patrice Lerouge, Loïc Faye, and Louis-P. Vézina
Subjects: Glycan, medicine.drug_class, fungi, food and beverages, Plant Science, Biology, Monoclonal antibody, Epitope, In vitro, law.invention, carbohydrates (lipids), Biochemistry, N-linked glycosylation, law, Recombinant DNA, biology.protein, medicine, Plantibody, Antibody, Agronomy and Crop Science, Biotechnology
Abstract: Structural analysis of the N-glycosylation of alfalfa proteins was investigated in order to evaluate the capacity of this plant to perform this biologically important post-translational modification. We show that, in alfalfa, N-linked glycans are processed into a large variety of mature oligosaccharides having core-xylose and core alpha(1,3)-fucose, as well as terminal Lewis(a) epitopes. In contrast, expression of the C5-1 monoclonal antibody in alfalfa plants results in the production of plant-derived IgG1 which is N-glycosylated by a predominant glycan having a alpha(1,3)-fucose and a beta(1,2)-xylose attached to a GlcNAc2Man3GlcNAc2 core. Since this core is common to plant and mammal N-linked glycans, it therefore appears that alfalfa plants have the ability to produce recombinant IgG1 having a N-glycosylation that is suitable for in vitro or in vivo glycan remodelling into a human-compatible plantibody. For instance, as proof of concept, in vitro galactosylation of the alfalfa-derived C5-1 mAb resulted in a homogenous plantibody harbouring terminal beta(1,4)-galactose residues as observed in the mammalian IgG.
Published: 2003
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26. Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas aeruginosa PA14 strain

Author: Thierry Jouenne, Tassadit Ouidir, Pascal Cosette, Frédérique Jarnier, and Julie Hardouin
Subjects: inorganic chemicals, Molecular Sequence Data, Virulence, Biology, medicine.disease_cause, Biochemistry, Mass Spectrometry, Microbiology, Serine, Bacterial Proteins, Extracellular, medicine, Protein phosphorylation, Amino Acid Sequence, Threonine, Amino Acids, Phosphorylation, Molecular Biology, Pseudomonas aeruginosa, Membrane Proteins, Phosphoproteins, enzymes and coenzymes (carbohydrates), Signal transduction, Extracellular Space
Abstract: Protein phosphorylation on serine, threonine, and tyrosine is known to be involved in a wide variety of cellular processes, signal transduction, and bacterial virulence. We characterized, for the first time, the extracellular phosphoproteins of the Pseudomonas aeruginosa PA14 strain. We identified 28 phosphoproteins (59 phosphosites) including enzymes, with various phosphorylation sites, known as potent secreted virulence factors in P. aeruginosa. The high phosphorylation level of these virulence factors might reflect a relationship between Ser/Thr/Tyr phosphorylation and virulence.
Published: 2014

27. Antiviral effects of polyphenols: development of bio-based cleaning wipes and filters

Author: Laurent Lebrun, Pascal Cosette, Manuella Catel-Ferreira, Hédia Tnani, Claire Hellio, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), University of Portsmouth, Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Polyphenol, viruses, 02 engineering and technology, medicine.disease_cause, Antiviral Agents, Virus, Catechin, Microbiology, law.invention, Bacteriophage, 03 medical and health sciences, chemistry.chemical_compound, law, Virology, medicine, [CHIM]Chemical Sciences, Bacteriophage T4, Cellulose, Escherichia coli, Filtration, 030304 developmental biology, Laccase, 0303 health sciences, Chromatography, Microbial Viability, biology, Mask, Filter, ACL, Masks, Chemical modification, Polyphenols, Wipes, [CHIM.MATE]Chemical Sciences/Material chemistry, Viral Load, 021001 nanoscience & nanotechnology, biology.organism_classification, 3. Good health, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Disinfection, [CHIM.POLY]Chemical Sciences/Polymers, chemistry, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, 0210 nano-technology, Disinfectants
Abstract: International audience; Polyphenol molecules play multiple essential roles in plant physiology such as defences against plant-pathogens and micro-organisms. The present study reports a chemical modification of the surface of non-woven cellulosic fibre filters (Kimwipes (R)) by fixing polyphenol in order to confer them antiviral properties. The grafting of the non-woven fibres by the antiviral entity was performed using laccase. T4D bacteriophage virus of Escherichia coli B was used as virus model. Catechin polyphenol was tested as antiviral entity. Proteomic experiments were performed to quantify the potential protein target of catechin on viruses. When the modified filter was in contact with the viral suspension a large improvement in the reduction of the viral concentration was observed (5-log after 1 h). Thus, we propose that this material could be used as virucidal wipes for the virus elimination from contaminated surfaces. Virus filtration experiments were performed by spraying an aerial suspension of T4D bacteriophage virus through the designed filter. The best virus capture factor f (ratio of upstream to downstream virus contents) was obtained when using 2 functionalized filters (f = 2.9 x 10(3)). When these 2 layers were placed inside a commercial medical mask in place of its cellulose layer (Kolmi M24001 mask) (f = 3.5 x 10(4)), the f ratio then reached 2.6 x 10(5) for 2 h of filtration. Based on these results, this novel bio-based antiviral mask represents a significant improvement over conventional medical masks.
Published: 2014
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28. Growth Retardation, Reduced Invasiveness, and Impaired Colistin-Mediated Cell Death Associated with Colistin Resistance Development in Acinetobacter baumannii

Author: Athanassios Tsakris, Spyros Pournaras, Emmanuelle Dé, Yassine Nait Chabane, Julie Hardouin, Aggeliki Poulou, Ioulia Kristo, Konstantina Dafopoulou, Pascal Cosette, Demosthenes Makris, Department of Microbiology, University of Thessaly [Volos] (UTH), Serres General Hospital, Intensive Care Unit, University of Thessaly [Volos] (UTH)-University Hospital of Larisa, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), National and Kapodistrian University of Athens (NKUA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), and Normandie Université (NU)
Subjects: Acinetobacter baumannii, medicine.drug_class, [SDV]Life Sciences [q-bio], Antibiotics, Microbial Sensitivity Tests, Drug resistance, medicine.disease_cause, Microbiology, Superoxide dismutase, Bacterial Proteins, Mechanisms of Resistance, Drug Resistance, Bacterial, Operon, medicine, Humans, [CHIM]Chemical Sciences, Pharmacology (medical), ComputingMilieux_MISCELLANEOUS, Aged, Antibacterial agent, Aconitate Hydratase, Pharmacology, Microbial Viability, biology, Colistin, Superoxide Dismutase, Pseudomonas aeruginosa, Gene Expression Regulation, Bacterial, Peroxiredoxins, biochemical phenomena, metabolism, and nutrition, Middle Aged, equipment and supplies, Catalase, biology.organism_classification, Anti-Bacterial Agents, Clone Cells, Infectious Diseases, biology.protein, Neisseriaceae, Acinetobacter Infections, medicine.drug
Abstract: Two colistin-susceptible/colistin-resistant (Col s /Col r ) pairs of Acinetobacter baumannii strains assigned to international clone 2, which is prevalent worldwide, were sequentially recovered from two patients after prolonged colistin administration. Compared with the respective Col s isolates (Ab248 and Ab299, both having a colistin MIC of 0.5 μg/ml), both Col r isolates (Ab249 and Ab347, with colistin MICs of 128 and 32 μg/ml, respectively) significantly overexpressed pmrCAB genes, had single-amino-acid shifts in the PmrB protein, and exhibited significantly slower growth. The Col r isolate Ab347, tested by proteomic analysis in comparison with its Col s counterpart Ab299, underexpressed the proteins CsuA/B and C from the csu operon (which is necessary for biofilm formation). This isolate also underexpressed aconitase B and different enzymes involved in the oxidative stress response (KatE catalase, superoxide dismutase, and alkyl hydroperoxide reductase), suggesting a reduced response to reactive oxygen species (ROS) and, consequently, impaired colistin-mediated cell death through hydroxyl radical production. Col s isolates that were indistinguishable by macrorestriction analysis from Ab299 caused six sequential bloodstream infections, and isolates indistinguishable from Ab248 caused severe soft tissue infection, while Col r isolates indistinguishable from Ab347 and Ab249 were mainly colonizers. In particular, a Col s isolate identical to Ab299 was still invading the bloodstream 90 days after the colonization of this patient by Col r isolates. These observations indicate considerably lower invasiveness of A. baumannii clinical isolates following the development of colistin resistance.
Published: 2014
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29. Overexpression of MHC class I in muscle of lymphocyte-deficient mice causes a severe myopathy with induction of the unfolded protein response

Author: François-Jérôme Authier, Olivier Boyer, Laurent Drouot, Manuel Fréret, Claire Dauly, Pascal Cosette, Antoine Obry, Sandra Ahmed-Lacheheb, and Sahil Adriouch
Subjects: T-Lymphocytes, Muscle Fibers, Skeletal, Intracellular Space, Muscle Proteins, chemical and pharmacologic phenomena, Mice, Transgenic, Human leukocyte antigen, Mice, SCID, Major histocompatibility complex, Pathology and Forensic Medicine, Myositis, Inclusion Body, Mice, Immune system, Muscular Diseases, MHC class I, medicine, Animals, Humans, Myopathy, biology, Muscles, Histocompatibility Antigens Class I, Acquired immune system, medicine.disease, Endoplasmic Reticulum Stress, Molecular biology, Immunohistochemistry, Cell biology, Up-Regulation, biology.protein, Unfolded Protein Response, Inclusion body myositis, medicine.symptom, CD8
Abstract: Muscle fibers do not normally express major histocompatibility complex class I (MHC-I) molecules, and their reexpression is a hallmark of inflammatory myopathies. It has been shown in mice that overexpression of MHC-I induces a poorly inflammatory myositis accompanied by the unfolded protein response (UPR), but it is unclear whether it is attributable to T-cell-mediated MHC-I-dependent immune responses or to MHC-I forced expression per se. Indeed, besides presenting antigenic peptides to CD8(+) T cells, MHC-I may also possibly exert nonimmunologic, yet poorly understood pathogenic effects. Thus, we investigated the pathogenicity of MHC-I expression in muscle independently of its immune functions. HT transgenic mice that conditionally overexpress H-2K(b) in muscle were bred to an immunodeficient Rag2(-/-) background. The muscle proteome was analyzed by label-free high-resolution protein quantitation and Western blot. Despite the absence of adaptive immunity, HT Rag2(-/-) mice developed a very severe myopathy associated with the cytoplasmic accumulation of H-2K(b) molecules. The UPR was manifest by up-regulation of characteristic proteins. In humans, we found that HLA class I molecules not only were expressed at the sarcolemma but also could accumulate intracellularly in some patients with inclusion body myositis. Accordingly, the UPR was triggered as a function of the degree of HLA accumulation in myofibers. Hence, reexpression of MHC-I in normally negative myofibers exerts pathogenic effects independently of its immune function.
Published: 2012

30. Antioxidative and DNA Protective Effects of Bacillomycin D-Like Lipopeptides Produced by B38 Strain

Author: Maria Luisa Mangoni, Imen Ben Slimene, Pascal Cosette, Olfa Tabbene, Ferid Limam, Salem Elkahoui, Dorra Gharbi, Mohamed Najib Alfeddy, Thierry Jouenne, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), and Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie)
Subjects: 0106 biological sciences, Antioxidant, Stereochemistry, medicine.medical_treatment, Iron, [SDV]Life Sciences [q-bio], Bioengineering, Free radicals, 01 natural sciences, Applied Microbiology and Biotechnology, Biochemistry, Lipopeptide, Lipid peroxidation, 03 medical and health sciences, chemistry.chemical_compound, Bacillomycin, Lipopeptides, 010608 biotechnology, Antioxidant compounds, medicine, Antifungal activity, Reactive oxygen species, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Superoxide, General Medicine, DNA, Free Radical Scavengers, 3. Good health, Amino acid, Culture Media, Oxidative Stress, chemistry, Hydroxyl radical, Lipid Peroxidation, Peptides, Biotechnology, Antimicrobial Cationic Peptides, DNA Damage
Abstract: In the present study, we evaluated the antioxidant and the scavenging ability of C14, C15 and C16 bacillomycin D-like lipopeptides produced by B38 strain. They all displayed strong reducing power activity, hydroxyl and superoxide anion radicals scavenging activities and inhibition of lipid peroxidation. In addition, they were found to protect plasmid DNA damage from hydroxyl radical oxidation. Data suggested that their antioxidant potency can be attributed to the hydrophobic and aromatic side-chain groups of their amino acids as well as to the aliphatic chain of their beta amino fatty acids. Note that the hydrocarbon chain length did not interfere with the antioxidant power. Overall, such bacillomycin D lipopeptides which exhibit antioxidant and radical scavenging activities may be useful for cosmetic, therapeutic or pharmaceutical purposes in order to delay or prevent oxidative deterioration of manufactured products.
Published: 2012
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31. Membrane proteomes of Pseudomonas aeruginosa and Acinetobacter baumannii

Author: Annick Schaumann, Stéphane Alexandre, Laurent Coquet, Thierry Jouenne, Bertrand Naudin, Christophe Rihouey, Axel Siroy, Emmanuelle Dé, A.C. Duncan, Guy-Alain Junter, Pascal Cosette, 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), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), CEA Le Ripault (CEA Le Ripault), Direction des Applications Militaires (DAM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), International Livestock Research Institute [CGIAR, Ethiopie] (ILRI), Consultative Group on International Agricultural Research [CGIAR] (CGIAR), Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), 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)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), and Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Acinetobacter baumannii, Proteomics, Proteome, Virulence, medicine.disease_cause, Microbiology, 03 medical and health sciences, Antibiotic resistance, Bacterial Proteins, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, medicine, Humans, Pseudomonas Infections, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, biology, 030306 microbiology, Pseudomonas aeruginosa, Chemistry, Membrane Proteins, General Medicine, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Membrane protein, Efflux, Bacterial outer membrane, Acinetobacter Infections
Abstract: Acinetobacter baumannii and Pseudomonas aeruginosa are known for their intrinsic resistance to antibiotics. Between mechanisms involved in this resistance, diminished expression of outer membrane proteins and up-regulation of efflux pumps play an important role. The characterization of membrane proteins is consequently necessary because of their importance in the antibiotic resistance but also in virulence. This review presents proteomic investigations aiming to describe the protein content of the membranes of these two bacterial species.
Published: 2011
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32. Triggering of the Antibacterial Activity of Bacillus subtilis B38 Strain against Methicillin-Resistant Staphylococcus aureus

Author: Maria Luisa Mangoni, Olfa Tabbene, Pascal Cosette, Najib Elfeddy, Ines Karkouch, Thierry Jouenne, Imen Ben Slimene, Ferid Limam, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Substances Bioactives (Centre de Biotechnologie de Borj Cedria, Hammam-Lif) (LSBA), and Centre de Biotechnologie de Borj Cédria (Hammam-Lif, Tunisie)
Subjects: Methicillin-Resistant Staphylococcus aureus, Hot Temperature, [SDV]Life Sciences [q-bio], Bioengineering, Microbial Sensitivity Tests, Bacillus subtilis, medicine.disease_cause, Applied Microbiology and Biotechnology, Biochemistry, Microbiology, 03 medical and health sciences, antibacterial activity, Bacterial Proteins, Antibiosis, medicine, induction, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Antibacterial agent, 0303 health sciences, biology, Strain (chemistry), 030306 microbiology, Chemistry, General Medicine, autoinducing compound, bacillus subtilis, mrsa, biology.organism_classification, Bacillales, Methicillin-resistant Staphylococcus aureus, Coculture Techniques, Anti-Bacterial Agents, Culture Media, Staphylococcus aureus, Electrophoresis, Polyacrylamide Gel, Antibacterial activity, Bacteria, Biotechnology
Abstract: When cultured in minimal growth medium, the B38 strain of Bacillus subtilis did not exhibit any antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA) clinical isolate. Coculturing B38 strain with viable MRSA cells weakly increased antibacterial activity production (20 AU/ml). Addition of dead MRSA cells in a B38 culture, increased by 8-fold the B. subtilis strain antibacterial activity reaching 160 AU/ml against MRSA strain. This antibacterial activity recovered from cell-free supernatants was stimulated by an autoinducing compound which is sensitive to the action of proteinase K suggesting a proteinaceous nature. This compound was heat-stable till 80 °C and showed a molecular mass around 20 kDa as determined by SDS-PAGE. These results suggest that the production of antibacterial compounds by B38 strain is dependent on the amount of the autoinducing compound.
Published: 2011
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33. Biofilm-induced modifications in the proteome of Pseudomonas aeruginosa planktonic cells

Author: David Vaudry, Thierry Jouenne, Anthony Collet, Guy-Alain Junter, Philippe Chan Tchi Song, Pascal Cosette, Hubert Vaudry, Yohan Nigaud, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Différenciation et communication neuronale et neuroendocrine (DC2N), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Neuroendocrinologie cellulaire et moléculaire
Subjects: Proteome, [SDV]Life Sciences [q-bio], Biophysics, Gene Expression, Biology, Reductase, medicine.disease_cause, Biochemistry, Analytical Chemistry, Microbiology, 03 medical and health sciences, Bioreactors, 4-Butyrolactone, Bacterial Proteins, Gene expression, medicine, Homoserine, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, 030306 microbiology, Pseudomonas aeruginosa, fungi, Biofilm, Quorum Sensing, Plankton, Quorum sensing, Alcohol Oxidoreductases, Oxidative Stress, Biofilms, 3-Oxoacyl-(Acyl-Carrier-Protein) Reductase, Autoinducer
Abstract: While recent studies focused on Quorum Sensing (QS) role in the cell-to-cell communication in free or biofilm cultures, no work has been devoted up to now to investigate the communication between sessile and planktonic bacteria. In this aim, we elaborated an original two-chambered bioreactor and used a proteomic approach to study the alterations induced by Pseudomonas aeruginosa biofilm cells on protein expression in planktonic counterparts (named SIPs for Surface-Influenced Planktonics). Proteomic analyses revealed the existence of 31 proteins whose amount varied in SIPs, among which five corresponded to hypothetic proteins and two (the Fur and BCP proteins) are involved in bacterial response to oxidative stress. An increase in the concentration of C(4)-HSL (rhlR-rhlI-dependent QS) and 3-oxo-C(12)-HSL (lasR-lasI-dependent QS) autoinducer molecules was shown in the planktonic compartment. Interestingly, among proteins that were accumulated by SIPs was 3-oxoacyl-[acyl-carrier-protein] reductase, a protein involved in the production of the autoinducer 3-oxo-C(12)-HSL. These results demonstrate that planktonic organisms are able to detect the presence of a biofilm in their close environment and to modify their gene expression in consequence.
Published: 2010
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34. Proteomic analysis of Staphylococcus aureus biofilms grown in vitro on mechanical heart valve leaflets

Author: Thierry Jouenne, Guy-Alain Junter, Jean-François Lemeland, Pascal Cosette, Laetitia Benard, Pierre-Yves Litzler, Service de chirurgie cadiovasculaire et thoracique [Rouen], Hôpital Charles Nicolle [Rouen]-CHU Rouen, Normandie Université (NU)-Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Staphylococcus aureus, Prosthesis-Related Infections, Proteome, [SDV]Life Sciences [q-bio], Cell, Biomedical Engineering, medicine.disease_cause, Mechanical heart-valve, Microbiology, Biomaterials, 03 medical and health sciences, Bacterial Proteins, medicine, Humans, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Leaflet (botany), biology, 030306 microbiology, Metals and Alloys, Biofilm, biology.organism_classification, Heart Valves, In vitro, medicine.anatomical_structure, Biofilms, Heart Valve Prosthesis, Ceramics and Composites, Bacteria
Abstract: The in vitro colonization of three commercial heart valve leaflets by Staphylococcus aureus was investigated. The leaflets, made of pyrolytic carbon alloyed with or without silicon, displayed similar surface properties (wettability, roughness) and were readily colonized by S. aureus that formed patchy biofilms on the three supports. A proteomic approach was used to assess the physiological status of biofilm populations by comparing their protein maps to those of bacteria cultured as free cells in the presence or absence of biofilm substratum. Principal component analysis (PCA) revealed, for each tested leaflet, statistical relationships between the protein maps of the biofilm and free-floating microbial populations. A spot-by-spot comparison of protein levels on two-dimensional electropherograms showed that many proteins were accumulated or underproduced by microbial populations grown in the presence of a leaflet compared with protein levels in control free populations. The number of accumulated proteins was noticeably higher than that of underproduced polypeptides. This protein overproduction was emphasized in biofilm populations. Several proteins, some of which were identified, were differentially produced by both surface-associated planktonic and biofilm-grown cell populations compared with control free-cell ones cultured in the absence of leaflet, whatever the leaflet tested. The potential of this proteomic approach for fighting against microbial adhesion and biofilm formation is discussed.
Published: 2009
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35. Identification of Biofilm-Associated Cluster (bac) in Pseudomonas aeruginosa Involved in Biofilm Formation and Virulence

Author: Alain Filloux, Camille Macé, Damien Seyer, Thierry Jouenne, Patrick Di-Martino, Virginie Molle, Chanez Chemani, Benoit Guery, Marc Fontaine, Guy-Alain Junter, Pascal Cosette, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Université Lille 2 - Faculté de Médecine, Biologie et physiologie des états septiques, IFR114-Université de Lille, Droit et Santé, MRC Centre for Molecular Microbiology and Infection [Imperial College, London] (CMBI), Imperial College London, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU), Institut de biologie et chimie des protéines [Lyon] (IBCP), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, The French Cystic Fibrosis Foundation (VLM), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), 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)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine Henri Warembourg - Université de Lille, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), and MOLLE, Virginie
Subjects: Male, Mutant, Outer membrane proteins, medicine.disease_cause, Bacterial Adhesion, Infectious Diseases/Bacterial Infections, Mice, Biochemistry/Protein Chemistry, Opportunistic infections, Phage shock, 0303 health sciences, Mice, Inbred BALB C, Multidisciplinary, Virulence, Microbiology/Immunity to Infections, Multidisciplinary Sciences, Multigene Family, Pseudomonas aeruginosa, Medicine, Science & Technology - Other Topics, Biological Assay, Microbiology/Cellular Microbiology and Pathogenesis, Research Article, Surface Properties, General Science & Technology, Science, Hypothetical protein, Molecular Sequence Data, Locus (genetics), Biology, Microbiology, 03 medical and health sciences, Bacterial Proteins, Osmotic Pressure, Cell Line, Tumor, MD Multidisciplinary, medicine, Animals, Humans, Pseudomonas Infections, Amino Acid Sequence, Mutant strains, Vascular permeability, Gene, DNA sequence analysis, 030304 developmental biology, Science & Technology, 030306 microbiology, Biofilm, Computational Biology, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Kinetics, Bacterial biofilms, Protein structure prediction, Genes, Bacterial, Biofilms, Mutation, Glycolipids, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Heat-Shock Response
Abstract: International audience; Biofilms are prevalent in diseases caused by Pseudomonas aeruginosa, an opportunistic and nosocomial pathogen. By a proteomic approach, we previously identified a hypothetical protein of P. aeruginosa (coded by the gene pA3731) that was accumulated by biofilm cells. We report here that a DpA3731 mutant is highly biofilm-defective as compared with the wild-type strain. Using a mouse model of lung infection, we show that the mutation also induces a defect in bacterial growth during the acute phase of infection and an attenuation of the virulence. The pA3731 gene is found to control positively the ability to swarm and to produce extracellular rhamnolipids, and belongs to a cluster of 4 genes (pA3729-pA3732) not previously described in P. aeruginosa. Though the protein PA3731 has a predicted secondary structure similar to that of the Phage Shock Protein, some obvious differences are observed compared to already described psp systems, e.g., this unknown cluster is monocistronic and no homology is found between the other proteins constituting this locus and psp proteins. As E. coli PspA, the amount of the protein PA3731 is enlarged by an osmotic shock, however, not affected by a heat shock. We consequently named this locus bac for biofilm-associated cluster.
Published: 2008
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36. Proteomic comparison of outer membrane protein patterns of sessile and planktonic Pseudomonas aeruginosa cells

Author: Damien Seyer, Christof Lenz, Hubert Vaudry, Emmanuelle Dé, Pascal Cosette, Laurent Coquet, Thierry Jouenne, Axel Siroy, Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), 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), Neuroendocrinologie cellulaire et moléculaire, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-CHU Rouen
Subjects: 0303 health sciences, 030306 microbiology, Pseudomonas aeruginosa, [SDV]Life Sciences [q-bio], Biofilm, Biology, medicine.disease_cause, Mass spectrometry, Applied Microbiology and Biotechnology, Phenotype, Microbiology, 03 medical and health sciences, Electrophoresis, medicine, Scanning densitometry, Bacterial outer membrane, Waste Management and Disposal, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology
Abstract: We have compared the outer membrane protein (OMP) pattern of sessile Pseudomonas aeruginosa cells with that of its stationary-phase free-floating counterparts. Two-dimensional electrophoretic gels were compared using computing scanning densitometry. The level of 103 OMPs (i.e. about 50% of the spots that fulfilled our statistical selection threshold) was significantly and reproducibly different in biofilm organisms as compared with their planktonic counterparts. Some OMPs that specifically either accumulated or decreased were identified by mass spectrometry and the role of these proteins in the biofilm phenotype is discussed.
Published: 2005
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37. Comparative proteomic analysis of planktonic and immobilized Pseudomonas aeruginosa cells: a multivariate statistical approach

Author: Sébastien Vilain, Guy-Alain Junter, Thierry Jouenne, Marie Hubert, Pascal Cosette, Catherine Lange, Biotechnologie des protéines recombinantes à visée santé, Université de Bordeaux (UB)-Institut Polytechnique de Bordeaux, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Spectrométrie de Masse Bio-organique [Rouen], Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Proteomics, Proteome, [SDV]Life Sciences [q-bio], Biophysics, medicine.disease_cause, Biochemistry, Matrix (chemical analysis), 03 medical and health sciences, Bacterial Proteins, medicine, Electrophoresis, Gel, Two-Dimensional, Molecular Biology, Incubation, Cells, Cultured, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Chromatography, biology, 030306 microbiology, Pseudomonas aeruginosa, Biofilm, Cell Biology, Plankton, biology.organism_classification, Electrophoresis, Cell culture, Biofilms, Principal component analysis, Bacteria
Abstract: The protein maps of Pseudomonas aeruginosa cells from two natural (attached) and one artificial (gel-entrapped) immobilized-cell (IC) systems, together with their free (suspended) counterparts, were compared after incubation for 18 or 48 h in a minimal salt medium. Principal component analysis (PCA) was used to interpret the variations in protein spot densities that were observed on electropherogram obtained by two-dimensional electrophoresis (2-DE). PCA of the 2-DE data, a matrix of 933 rows (observations, i.e., spot density values) and 12 columns (variables, i.e., incubation conditions), in which observations were standardized horizontally, extracted four principal components (PCs) accounting for 78.75% of the variability in the protein expression profiles. PC1 opposed the two modes of growth (planktonic and immobilized) while PC2 discriminated between the incubation times of free cell cultures. The incubation conditions of ICs, including the immobilization procedure (entrapment vs attachment) and the nature of the biofilm substratum, were fairly separated in PC3 × PC4. The dependence of the protein patterns on the cell immobilization process was further illustrated by the identification of a number of peptides whose amount remained unchanged or was altered in ICs compared to free bacteria. These results reinforce the topical assertion that bacteria in the immobilized state display a specific physiological behavior but also question the existence of a unique IC phenotype.
Published: 2004
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38. Biofilm Proteome: Homogeneity or Versatility?

Author: Jean-Paul Dupont, Thierry Jouenne, Pascal Cosette, Sébastien Vilain, Guy-Alain Junter, Irène Zimmerlin, Biotechnologie des protéines recombinantes à visée santé, Université de Bordeaux (UB)-Institut Polytechnique de Bordeaux, Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Morphodynamique Continentale et Côtière (M2C), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), and Normandie Université (NU)-Université Le Havre Normandie (ULH)
Subjects: Surface Properties, proteome, [SDV]Life Sciences [q-bio], Biology, medicine.disease_cause, Biochemistry, biofilm, Microbiology, 03 medical and health sciences, Bacterial Proteins, medicine, Cell Adhesion, Electrophoresis, Gel, Two-Dimensional, Cell adhesion, 030304 developmental biology, Gel electrophoresis, 0303 health sciences, 030306 microbiology, Pseudomonas aeruginosa, Biofilm, General Chemistry, biochemical phenomena, metabolism, and nutrition, Antimicrobial, biology.organism_classification, Plankton, Phenotype, multivariate analysis, P. aeruginosa, Biofilms, Proteome, Microscopy, Electron, Scanning, Gels, Bacteria
Abstract: International audience; The problems associated with biofilm infections in humans result from the distinct characteristics of biofilms, in particular their high level of resistance to antibiotics. One of the hypotheses that have been advanced to explain this resistance to antimicrobials is the phenotypic differentiation of biofilm cells. Although many studies on biofilms have highlighted physiological alterations following the attachment of bacteria to a surface, no studies have explicitly demonstrated a “biofilm” physiology. To contribute to this topical debate, we used principal component analysis to interpret spot quantity variations observed on electropherograms obtained by two-dimensional gel electrophoresis of crude protein extracts from planktonic and sessile Pseudomonas aeruginosa cells. These analyses showed that the proteome of attached P. aeruginosa cells differs from that of their planktonic counterparts. Furthermore, we found that the proteome of sessile P. aeruginosa is strongly dependent on the nature of the biofilm substratum.
Published: 2004
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39. Occurrence and phenotypic characterization of Yersinia ruckeri strains with biofilm-forming capacity in a rainbow trout farm

Author: Laurent Quillet, Laurent Coquet, Thierry Jouenne, Fabienne Petit, Pascal Cosette, G-A Junter, Polymères Biopolymères Surfaces (PBS), 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)-Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-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)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Microbiologie du Froid, Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Institut Fédératif de Recherches Multidisciplinaires sur les Peptides (IFRMP 23), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Lutte Contre le Cancer Henri Becquerel Normandie Rouen (CLCC Henri Becquerel)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Université Le Havre Normandie (ULH), and Normandie Université (NU)-CHU Rouen
Subjects: Yersinia Infections, Fish farming, [SDV]Life Sciences [q-bio], Molecular Sequence Data, Colony Count, Microbial, Fisheries, Microbial Sensitivity Tests, Yersinia, Applied Microbiology and Biotechnology, Polymerase Chain Reaction, Bacterial Adhesion, Microbiology, 03 medical and health sciences, Fish Diseases, Oxolinic acid, medicine, Animals, Environmental Microbiology and Biodegradation, Amino Acid Sequence, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Ecology, biology, 030306 microbiology, Biofilm, Eukaryota, biology.organism_classification, DNA Fingerprinting, Anti-Bacterial Agents, Phenotype, Biofilms, Oncorhynchus mykiss, Rainbow trout, Yersinia ruckeri, Water Microbiology, Bacteria, Food Science, Biotechnology, medicine.drug, Bacterial Outer Membrane Proteins
Abstract: The presence of Yersinia ruckeri in a French fish farm was investigated. Y. ruckeri was isolated mainly from algae and sediment samples rather than from water. Twenty-two Y. ruckeri isolates were obtained, and three strains were distinguished by enterobacterial repetitive intergenic consensus PCR amplification. These strains were able to adhere to solid supports. This characteristic was correlated with flagellum-mediated motility. Killing experiments showed that sessile cells were more resistant to oxolinic acid than their planktonic counterparts. Our results demonstrate that surface colonization of fish farm tanks by Y. ruckeri biofilms is a potential source of recurrent infection for extended periods of time.
Published: 2002
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40. Identification of S100A9 as Biomarker of Responsiveness to the Methotrexate/Etanercept Combination in Rheumatoid Arthritis Using a Proteomic Approach

Author: Olivier Boyer, Pascal Cosette, Peggy Philippe, Antoine Obry, Patrice Fardellone, Thierry Lequerré, Olivier Vittecoq, Xavier Le Loët, and Julie Hardouin
Subjects: Male, Proteomics, lcsh:Medicine, Arthritis, Pharmacology, Biochemistry, Biomarkers, Pharmacological, Receptors, Tumor Necrosis Factor, Mass Spectrometry, Etanercept, Analytical Chemistry, Arthritis, Rheumatoid, Cohort Studies, Spectrum Analysis Techniques, Medicine and Health Sciences, Medicine, lcsh:Science, Multidisciplinary, Middle Aged, Drug Combinations, Chemistry, Antirheumatic Agents, Rheumatoid arthritis, Physical Sciences, Biomarker (medicine), Female, Research Article, medicine.drug, Adult, Immunology, Rheumatoid Arthritis, Research and Analysis Methods, Peripheral blood mononuclear cell, S100A9, Autoimmune Diseases, S100A8, Young Adult, Rheumatology, Calgranulin B, Humans, Calgranulin A, Aged, business.industry, lcsh:R, Biology and Life Sciences, medicine.disease, Methotrexate, Immunoglobulin G, Leukocytes, Mononuclear, Clinical Immunology, lcsh:Q, Calprotectin, business, Leukocyte L1 Antigen Complex, Biomarkers
Abstract: Objectives One way to optimize the drug prescription in rheumatoid arthritis (RA) is to identify predictive biomarkers of drug responsiveness. Here, we investigated the potential "theranostic" value of proteins of the S100 family by monitoring levels of both S100A8 and S100A9 in blood samples from RA patients. Design For proteomic analysis, peripheral blood mononuclear cells (PBMC) and serum samples were collected in patients prior to initiation of the methotrexate/etanercept (MTX/ETA) combination. Firstly, relative mass spectrometry (MS) quantification focusing on S100A8 and S100A9 proteins was carried out from PBMCs samples to identify potential biomarkers. The same approach was also performed from serum samples from responder (R) and non responder (NR) patients. Finally, to confirm these results, an absolute quantification of S100A8, S100A9 proteins and calprotectin (heterodimer of S100A8/S100A9) was carried out on the serum samples using ELISA. Results MS analyses revealed that both S100A8 and S100A9 proteins were significantly accumulated in PBMC from responders. In contrast to PBMC, only the S100A9 protein was significantly overexpressed in the serum of R patients. Absolute quantification by ELISA confirmed this result and pointed out a similar expression level of S100A8 protein and calprotectin in sera from both R and NR groups. Thus, the S100A9 protein revealed to be predictive of MTX/ETA responsiveness, contrarily to parameters of inflammation and auto-antibodies which did not allow significant discrimination. Conclusion This is the first report of an overexpression of S100A9 protein in both PBMCs and serum of patients with subsequent response to the MTX/ETA combination. This protein thus represents an interesting biomarker candidate of therapeutic response in RA.
Published: 2014
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41. A9.5 Identification and Validation of a Protein Combination Including S100A9 able to Predict the Response to the MTX/Etanercept Association in Rheumatoid Arthritis Patients

Author: A Obry, Julie Hardouin, Olivier Vittecoq, Thierry Lequerré, Olivier Boyer, and Pascal Cosette
Subjects: Oncology, medicine.medical_specialty, education.field_of_study, business.industry, Immunology, Population, medicine.disease, Connective tissue disease, Blood proteins, Peripheral blood mononuclear cell, General Biochemistry, Genetics and Molecular Biology, Etanercept, Rheumatology, Internal medicine, Rheumatoid arthritis, Proteome, medicine, Immunology and Allergy, Methotrexate, education, business, medicine.drug
Abstract: Background The number of biologic agents in Rheumatoid Arthritis (RA) is continuously increasing. However, clinicians observe that around 30 to 40% of treated patients fail to respond to TNFα blocking agents. One way to optimise the drug prescription is to identify predictive markers of drug responsiveness. Objectives To identify a combination of serum proteins whose expression profile would predict the RA patients responses to the association of methotrexate (MTX) and etanercept (ETA) by mass spectrometry-based quantification methods and ELISA. Methods A “cohort discovery phase” of 23 patients with active RA was treated by a subcutaneous injection of. The clinical efficacy of these drugs was evaluated with the DAS28 score after 6 months of treatment according to the EULAR response criteria. For proteomic analysis, a serum sample was collected in patients prior to treatment exposure. A “label free” approach on the whole proteome was performed by mass spectrometry on the 25 sera. Accordingly, the proteome of each sample was extracted and in-gel digested. The resulting peptides were analysed by LTQ Orbitrap® (ThermoFisher). Differential analysis between responder and non responder samples was performed with LCMS ProGenesis® (Nonlinear Dynamics). To validate these results a relative quantification of selected protein was performed on the second “cohort validation phase” by ELISA. The proteome of peripheral blood mononuclear cells (PBMC) from a second cohort of seven patients with similar characteristics has also been studied by the same label free approach. Results The label free approach revealed 12 differentially expressed serum proteins according to patient response. This combination of proteins was used to build a Random Forest statistical model to predict the patient’s status. This model was validated by a blind test on a panel of seven patients. Moreover, these results have shown the protein S100A9 overexpression in both the serum and the PBMCs from responder’s patients and this expression was confirmed by ELISA. Conclusions The label free approach has identified a combination of predictive markers of response to MTX treatment/ETA. Thus, using sera samples collected in patients prior to treatment exposure, it is possible to predict response to treatment with a small error. These proteins represent interesting candidate biomarkers of response that must be validated in a larger population. Already identified as a diagnostic and prognostic biomarker of RA, the S100A9 protein has been identified as a predictive biomarker of response both in serum and in PBMCs.
Published: 2013
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42. Identification of a set of eight proteins able to predict the response to methotrexate/etanercept in rheumatoid arthritis patients

Author: P. Morel, Pascal Cosette, P. Fardellone, P Chan Tchi Tsong, C Dauly, R.M. Flipo, X. Le Loët, Olivier Vittecoq, Antoine Obry, Thierry Lequerré, J Siemowski, Olivier Boyer, and Christian Marcelli
Subjects: Oncology, medicine.medical_specialty, education.field_of_study, business.industry, Immunology, Population, Quantitative proteomics, Orbitrap, medicine.disease, Peripheral blood mononuclear cell, General Biochemistry, Genetics and Molecular Biology, law.invention, Etanercept, Subcutaneous injection, Rheumatology, law, Internal medicine, Rheumatoid arthritis, medicine, Immunology and Allergy, Methotrexate, education, business, medicine.drug
Abstract: Background The number of biologic agents in rheumatoid arthritis (RA) is continuously increasing. However, clinicians observe that around 30–40% of treated patients fail to respond to tumour necrosis factor α blocking agents. One way to optimise the drug prescription is to identify predictive markers of drug responsiveness. Objectives To identify a combination of proteins whose expression profile would predict the RA patients responses to the association of methotrexate (MTX) and etanercept (ETA). Methods A set of 10 patients with active RA (average age: 54±16 years old, RA duration: 9±9 years, MTX: 18±3 mg/week, DAS28: 5.5±1.0) was treated by a subcutaneous injection of ETA (50 mg/week). The clinical efficacy of these drugs was evaluated with the DAS28 score after 3, 6 and 12 months of treatment according to the EULAR response criteria. For proteomic analysis, a blood sample was carried out in patients prior to the first injection in order to extract peripheral blood mononuclear cells (PBMC). A relative quantification of protein expression from seven samples of PBMC was performed by mass spectrometry, after labelling with stable isotopes (Isobaric Tags for Relative and Absolute Quantification: iTRAQ). Protein identification and differential analysis between the samples from responders (R) and non-responders (NR) were made with the Spectrum Mill software (Agilent). The statistical treatment using iQuantitator has enabled the relative protein quantification for each patient. From five others samples of PBMC, a complementary approach based exclusively on mass spectrometry was implemented (the ‘label free approach’). ‘Label-free’ quantification is based on extracted ion chromatograms to determine the differential expression. The differential analysis was achieved with SIEVE (Thermofisher), a label-free dedicated software to compare LC/MS data from LTQ Orbitrap (Thermofisher) analysis. Results Among the 10 patients, 6 out of 10 were classified as R. When merging the two independent experimental approaches, the authors got consistent results for eight overexpressed proteins and two underexpressed proteins among all patients responding to treatment. Conclusions For the first time, the authors identified a proteomic signature from PBMC able to predict MTX/ETA response. These proteins would thus represent valuable candidates for biomarkers of response to this treatment option that should be validated on a larger population. In addition, among the identified proteins, several proteins are also present in plasma, offering the possibility to explore their predictive value by ELISA tests.
Published: 2012
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43. Mitigation of monocyte driven thrombosis on cobalt chrome surfaces in contact with whole blood by thin film polar/hydrophobic/ionic polyurethane coatings

Author: Mohamed Amine Ben Mlouka, Véronique Regnault, Didier Letourneur, Adeline Gand, Pascal Cosette, Emmanuel Pauthe, J. Paul Santerre, Audrey Gossart, Véronique Ollivier, Univ Paris Diderot, INSERM, Lab Vasc Translat Sci U1148, Paris, France, Laboratoire de Recherche Vasculaire Translationnelle (LVTS (UMR_S_1148 / U1148)), Université Paris Diderot - Paris 7 (UPD7)-Université Paris 13 (UP13)-Institut National de la Santé et de la Recherche Médicale (INSERM), Equipe de recherche sur les relations matrice extracellulaire-cellules (ERRMECe), Fédération INSTITUT DES MATÉRIAUX DE CERGY-PONTOISE (I-MAT), Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine-Université de Cergy Pontoise (UCP), Université Paris-Seine-Université Paris-Seine, Institute of Biomaterials and Biomedical Engineering [Ontario, Canada] (IBBME), University of Toronto, Défaillance Cardiovasculaire Aiguë et Chronique (DCAC), Centre Hospitalier Régional Universitaire de Nancy (CHRU Nancy)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL), Plate-forme de Protéomique PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Rouen Normandie (UNIROUEN), and Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: MESH: Inflammation, [SDV]Life Sciences [q-bio], Polyurethanes, 02 engineering and technology, Fibrinogen, MESH: Monocytes, Monocytes, MESH: Polyurethanes, MESH: Thrombin, Coated Materials, Biocompatible, MESH: Coated Materials, Biocompatible, MESH: Fibrin, ComputingMilieux_MISCELLANEOUS, Whole blood, Principal Component Analysis, 0303 health sciences, biology, Chemistry, MESH: Hydrophobic and Hydrophilic Interactions, Thrombin, Biomaterial, 021001 nanoscience & nanotechnology, medicine.anatomical_structure, Coagulation, Mechanics of Materials, Inflammation Mediators, 0210 nano-technology, Hydrophobic and Hydrophilic Interactions, medicine.drug, Thrombin generation, MESH: Ions, Cobalt chrome, Surface Properties, MESH: Inflammation Mediators, Biophysics, Bioengineering, Fibrin, Thromboplastin, Biomaterials, 03 medical and health sciences, Tissue factor, MESH: Chromium Alloys, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, medicine, Humans, MESH: Cell Shape, MESH: Thrombosis, Cell Shape, 030304 developmental biology, Inflammation, Ions, MESH: Principal Component Analysis, MESH: Surface Properties, MESH: Humans, Tumor Necrosis Factor-alpha, Macrophages, Monocyte, MESH: Macrophages, Thrombosis, Polyurethane films, MESH: Thromboplastin, Fibronectin, MESH: Tumor Necrosis Factor-alpha, Ceramics and Composites, biology.protein, Chromium Alloys
Abstract: International audience; Monocytes are active at the crossroads between inflammation and coagulation processes since they can secrete pro-inflammatory cytokines and express tissue factor (TF), a major initiator of coagulation. Cobalt-chrome (CoCr), a metal alloy, used as a biomaterial for vascular stents, has been shown to be potentially pro-thrombotic and pro-inflammatory. Research work with a polymer from a family of degradable-polar hydrophobic ionic polyurethanes (D-PHI), called HHHI, has been shown to exhibit anti-inflammatory responses from human monocytes. We have generated multifunctional polyurethane thin films (MPTF) based on the HHHI chemistry, as a thin coating for CoCr and have evaluated the reactivity of blood with MPTF-coated CoCr. The results showed that the coating of CoCr with MPTF derived from HHHI prevents thrombin generation, reduces coagulation activation, and suppresses fibrin formation in whole blood. Activation of monocytes was also suppressed at the surface of MPTF-coated CoCr and specifically the decrease in thrombin generation was accompanied by a significant decrease in TF and pro-inflammatory cytokine levels. Mass spectroscopy of the adsorbed proteins showed lower levels of fibrinogen, fibronectin and complement C3, C4, and C8 when compared to CoCr. We can conclude that MPTFs reduce the pro-thrombotic and pro-inflammatory phenotype of monocytes and macrophages on CoCr, and prevent clotting in whole blood.
Published: 1970
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