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1. Sequence variability and phylogenetic analyses of the Complement Regulatory Protein expressed by the trypomastigote stage of Trypanosoma cruzi identify a monophyletic group of CRP-like proteins

Author

Mathieu-Daudé, Françoise, Lafay, Bénédicte, Touzet, Olivia, Bosseno, Marie-France, Parrado, Favio, Rojas, Ana Maria, Brenière, Simone Frédérique, UR008 Pathogénie des Trypanosomatidés (IRD), Institut de Recherche pour le Développement (IRD [France-Sud]), Génétique et évolution des maladies infectieuses (GEMI), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [France-Sud]), Muscle et pathologies, Université Montpellier 1 (UM1)-IFR3, Université Montpellier 1 (UM1)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM), UMA de Pneumologie, Centre Hospitalier du Val d?Ariège, and Spanish National Cancer Research Center (CNIO)

Subjects
FL-160, Trypanosoma cruzi, [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE], trans-sialidase-like proteins, complement regulatory protein, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
Abstract

National audience; The complement regulatory protein (CRP) of Trypanosoma cruzi is a surface glycoprotein that confers to the infectious trypomastigote forms a protection against the lytic activity of the host complement. To define better the CRP within the large family of trans-sialidase-like proteins, we investigated the CRP sequence diversity in the trypomastigote stage of several T. cruzi strains and used a phylogenetic analysis based on the amino acid alignment of the CRP with the 200 top scoring proteins detected through a database sequence homology search. Intrastrain variations revealed the presence of several different CRP transcripts per strain and the interstrain variability was consistent with the subdivision of T. cruzi into genetic lineages. The phylogenetic analysis including the putative proteins retrieved from the T. cruzi genome project database did not differentiate the CRP from the FL-160 proteins and clustered them into a monophyletic group characterized by the presence of the 12 amino acid mimicry epitope that shows cross-reactivity with nervous tissues. In turn, proteins of this group did not bear classical complement control protein modules involved in C3b/C4b binding. The high sequence similarity observed in this group of CRP-like proteins opens up new prospects for the exploration of their functional diversity or similarity and their involvement in the resistance to the complement. This study provides information for the T. cruzi genome annotation of the trans-sialidase-like putative proteins

Published
2008

2. Exploring the FL-160-CRP gene family through sequence variability of the complement regulatory protein (CRP) expressed by the trypomastigote stage of Trypanosoma cruzi

Author

Olivia Touzet, Ali Ouaissi, Favio Parrado, Marie-France Bosseno, Salima Fatha, Joël Lelièvre, Simone Frédérique Brenière, Ana M. Rojas, Françoise Mathieu-Daudé, Bénédicte Lafay, UR008 Pathogénie des Trypanosomatidés (IRD), Institut de Recherche pour le Développement (IRD [France-Sud]), Génétique et évolution des maladies infectieuses (GEMI), Université Montpellier 1 (UM1)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Muscle et pathologies, Université Montpellier 1 (UM1)-IFR3, Université Montpellier 1 (UM1)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de chimie de coordination (LCC), Institut de Chimie de Toulouse (ICT-FR 2599), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), UMA de Pneumologie, Centre Hospitalier du Val d?Ariège, Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Institut de Recherche pour le Développement (France), Institut National de la Santé et de la Recherche Médicale (France), Centre National de la Recherche Scientifique (CNRS)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD [France-Sud]), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Spanish National Cancer Research Center (CNIO), Dynamique des interactions membranaires normales et pathologiques (DIMNP), and Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Amino Acid Motifs, Genes, Protozoan, MESH: Membrane Glycoproteins, Protozoan Proteins, MESH: Amino Acid Sequence, MESH: Amino Acid Motifs, 0302 clinical medicine, trans sialidase like proteins, Cluster Analysis, MESH: Animals, MESH: Genetic Variation, MESH: Phylogeny, MESH: Protozoan Proteins, Peptide sequence, Phylogeny, chemistry.chemical_classification, Genetics, 0303 health sciences, Membrane Glycoproteins, Multiple sequence alignment, MESH: Neuraminidase, Genome project, 3. Good health, Infectious Diseases, MESH: Genes, Protozoan, Multigene Family, MESH: Trypanosoma cruzi, Microbiology (medical), Trypanosoma cruzi, Molecular Sequence Data, 030231 tropical medicine, MESH: Glycoproteins, Neuraminidase, Biology, Microbiology, 03 medical and health sciences, FL 160, Phylogenetics, Genetic variation, Animals, Gene family, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, MESH: Life Cycle Stages, Molecular Biology, Ecology, Evolution, Behavior and Systematics, Glycoproteins, 030304 developmental biology, Life Cycle Stages, MESH: Molecular Sequence Data, FL-160, Trans-sialidase-like proteins, Genetic Variation, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, biology.organism_classification, MESH: Cluster Analysis, chemistry, Complement regulatory protein, MESH: Multigene Family, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, Glycoprotein
Abstract

The complement regulatory protein (CRP) of Trypanosoma cruzi is a surface glycoprotein which confers to the infectious trypomastigote forms a protection against the lytic activity of the host complement. CRP belongs to the large family of the trans-sialidase-like proteins and its sequence is highly similar to those of the flagellar FL-160 and chronic exoantigen proteins, encoded by a multigene family. To further define the gene family encoding the CRP, we investigated the protein diversity among several strains of T. cruzi through the sequencing of trypomastigote transcripts, and used a phylogenetic analysis based on the multiple alignment of these proteins with the top scoring sequences detected by a database sequence homology search. Intrastrain variations in CRP sequences revealed the existence of several copies per strain. The interstrain variability of CRP was consistent with the genetic subdivisions of T. cruzi into lineages and discrete typing units. The phylogenetic analysis based on a 227 amino acid alignment of CRP sequences with the 200 putative proteins retrieved from the protein databases (including the sequences from the T. cruzi genome project) revealed that the CRP sequences clustered with the FL-160 proteins into a monophyletic group characterized by the presence of the 12 amino acid mimicry epitope that mimics nervous tissues. The phylogeny did not differentiate between the CRP and the FL-160 proteins. The identification of this group of CRP-like proteins and the high sequence similarity observed within it open up new prospects for the exploration of the localization, structure and function of these proteins and a better understanding of their involvement in key aspects of host–parasite interactions, such as the resistance to the complement. This work provides also information for the T. cruzi genome annotation of the trans-sialidase-like putative proteins., These investigations received financial support from the “Institut de Recherche pour le Développement” (IRD), the “Institut National de la Santé et de la Recherche Médicale” (INSERM), and the French National Programme “ACI Microbiologie” Contract No. MIC 03 29.

Published
2008
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3. Sequence diversity and differential expression of Tc52 immuno-regulatory protein in Trypanosoma cruzi: potential implications in the biological variability of strains

Author

Ali Ouaissi, Denis Sereno, Joël Lelièvre, Françoise Mathieu-Daudé, Marie-France Bosseno, Edwin Garzon, Simone Frédérique Brenière, UR008 Pathogénie des Trypanosomatidés (IRD), Institut de Recherche pour le Développement (IRD [France-Sud]), UMA de Pneumologie, Centre Hospitalier du Val d?Ariège, Laboratoire de chimie de coordination (LCC), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Immunologie clinique, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Groupe Henri-Mondor Albert-Chenevier, Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie de Toulouse (ICT-FR 2599), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Sequence Analysis, DNA, Protozoan Proteins, MESH: Amino Acid Sequence, Virulence factor, MESH: Protein Structure, Tertiary, 0302 clinical medicine, MESH: Animals, MESH: Genetic Variation, MESH: Protozoan Proteins, Genetics, Regulation of gene expression, 0303 health sciences, biology, Kinetoplastida, General Medicine, MESH: Amino Acid Substitution, Infectious Diseases, Biochemistry, MESH: RNA, Protozoan, MESH: Trypanosoma cruzi, RNA, Protozoan, Trypanosoma cruzi, 030231 tropical medicine, Molecular Sequence Data, MESH: Sequence Alignment, MESH: DNA, Protozoan, Virulence, 03 medical and health sciences, Phylogenetics, MESH: Polymorphism, Genetic, parasitic diseases, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, RNA, Messenger, MESH: RNA, Messenger, 030304 developmental biology, MESH: Molecular Sequence Data, Binding Sites, Polymorphism, Genetic, General Veterinary, Genetic Variation, Sequence Analysis, DNA, DNA, Protozoan, biology.organism_classification, Protein Structure, Tertiary, MESH: Binding Sites, Amino Acid Substitution, Insect Science, Parasitology, Glutathione binding, Sequence Alignment, Function (biology)
Abstract

International audience; Trypanosoma cruzi is highly heterogeneous in terms of genetics and biological properties. To explore the diversity of T. cruzi, we focused our study on the T. cruzi Tc52 protein playing a critical immunosuppressive role during infection. Sequence variability and expression levels of this virulence factor were analysed in various strains. Among the 40 amino acid substitutions detected in the Tc52 coding sequences, three substitutions may have an impact on protein activity or function, as two are localized in sites involved in the glutathione binding and the third is present in the region bearing immunomodulatory function. This sequence variability was consistent with the genetic subdivisions of T. cruzi. Moreover, we observed that the level of Tc52 transcripts and proteins varied between the different strains, but we did not find a significant correlation between Tc52 expression and the phylogeny of the parasite. Thus, both diversity in the sequences and differences in the expression levels of Tc52 protein may be involved in the biological variability of T. cruzi, especially in virulence and immunosuppression properties of T. cruzi strains.

Published
2007
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