Chantal Rabourdin‐Combe

Inserm

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Denis Gerlier

Centre National de la Recherche Scientifique

Olga Azocar

Université Claude Bernard Lyon 1

Vincent Lotteau

Centre International de Recherche en Infectiologie

Pierre‐Olivier Vidalain

Université Claude Bernard Lyon 1

Marie-Claude Trescol-Biémont

Inserm

Christine Servet‐Delprat

Université Claude Bernard Lyon 1

Wolf H. Fridman

Centre de Recherche des Cordeliers

Branka Horvat

Centre International de Recherche en Infectiologie

Catheriné Sautès-Fridman

Centre de Recherche des Cordeliers

Patrick Bertolino

Centenary Institute

Cooperative Institutions

Inserm

181

Centre National de la Recherche Scientifique

166

Université Claude Bernard Lyon 1

120

École Normale Supérieure de Lyon

Centre International de Recherche en Infectiologie

Institut Pasteur

Université Paris Cité

Laboratoire de Biologie Moléculaire de la Cellule

Virologie et Pathologies Humaines

Hospices Civils de Lyon

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Substitution of peptide bond 53-54 of HEL(52-61) with an ethylene bond rather than reduced peptide bond is tolerated by an MHC-II restricted T cell.

HAL (Le Centre pour la Communication Scientifique Directe) (1996)

Laurent Ettouati Salvi Jp Trescol-Biémont Mc Nadia Walchshofer Denis Gerlier

To probe the interactions between major histocompatibility class-II molecules and the amide bonds of the antigenic peptide main chain, we synthesized ethylenic and reduced analogues of HEL(52-61), an immunogenic peptide for murine major histocompatibility class-II IA k restricted T-cell clones. The synthesis of the corresponding ethylenic analogue of HEL(52-61) in position 53-54 was performed by coupling the Fmoc-protected tripeptide Asp-Tyr-psi [E, CH = CH]Gly with HEL(55-61). Biological tests showed that the ethylenic peptide was presented by major histocompatibility class-II IA kappa molecule and recognized by HEL(52-61)-specific T-cell clones. The corresponding reduced peptide of HEL(52-61) at position 53-54 neither stimulated T-cell clones nor competed with the natural peptide. These results show that, while reduced pseudopeptides might not be appropriate, ethylenic pseudopeptides may be used as probes to dissect the role of hydrogen bonding between the peptide main chain and MHC residues and also help in the design of more stable immunogenic peptides.

Tripeptide

Peptide bond

Source

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Citations (10)

Measles Virus and Dendritic Cell Functions: How Specific Response Cohabits with Immunosuppression

Current topics in microbiology and immunology (2003)

Christine Servet‐Delprat Pierre‐Olivier Vidalain H. Valentin Chantal Rabourdin‐Combe

Immunosuppression

Priming (agriculture)

10.1007/978-3-662-06508-2_5

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Citations (58)

VirHostNet: a knowledge base for the management and the analysis of proteome-wide virus–host interaction networks

Nucleic Acids Research (2008)

Vincent Navratil Benoı̂t de Chassey Laurène Meyniel‐Schicklin Stéphane Delmotte Christian Gautier

Infectious diseases caused by viral agents kill millions of people every year. The improvement of prevention and treatment of viral infections and their associated diseases remains one of the main public health challenges. Towards this goal, deciphering virus–host molecular interactions opens new perspectives to understand the biology of infection and for the design of new antiviral strategies. Indeed, modelling of an infection network between viral and cellular proteins will provide a conceptual and analytic framework to efficiently formulate new biological hypothesis at the proteome scale and to rationalize drug discovery. Therefore, we present the first release of VirHostNet (Virus–Host Network), a public knowledge base specialized in the management and analysis of integrated virus–virus, virus–host and host–host interaction networks coupled to their functional annotations. VirHostNet integrates an extensive and original literature-curated dataset of virus–virus and virus–host interactions (2671 non-redundant interactions) representing more than 180 distinct viral species and one of the largest human interactome (10 672 proteins and 68 252 non-redundant interactions) reconstructed from publicly available data. The VirHostNet Web interface provides appropriate tools that allow efficient query and visualization of this infected cellular network. Public access to the VirHostNet knowledge-based system is available at http://pbildb1.univ-lyon1.fr/virhostnet.

Proteome

Interactome

Interaction network

10.1093/nar/gkn794

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Citations (150)

Conformational restriction of the Tyr⁵³ side‐chain in the decapeptide HEL[52‐61]: effects on binding to MHC‐II I‐A^k molecule and TCR recognition

Journal of Peptide Research (2000)

J. Richard Casimir Koen Iterbeke Wim Van Den Nest Dirk Tourwé Marie-Claude Trescol-Biémont

A series of conformationally restricted analogs of the hen egg lysozyme (HEL) decapeptide 52-61 in which the conformationally flexible Tyr53 residue was replaced by several more constrained tyrosine and phenylalanine analogs was prepared. Among these tyrosine and phenylalanine analogs were 1,2,3,4-tetrahydro-7-hydroxyisoquinoline-3-carboxylic acid (Htc), 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), 4-amino- 1,2,4,5-tetrahydro-8-hydroxy-2-benzazepine-3-one (Hba), 4-amino-1,2,4,5-tetrahydro-2-benzazepine-3-one (Aba), 2-amino-6-hydroxytetralin-2-carboxylic acid (Hat) and 2-amino-5-hydroxyindan-2-carboxylic acid (Hai) in which the rotations around Calpha-Cbeta and Cbeta-Cgamma were restricted because of cyclization of the side-chain to the backbone. Synthesis of Pht-Hba-Gly-OH using a modification of the Flynn and de Laszlo procedure is described. Analogs of beta-methyltyrosine (beta-MeTyr) in which the side-chains were biased to particular side-chain torsional angles because of substitution at the beta-hydrogens were also prepared. These analogs of HEL[52-61] peptide were tested for their ability to bind to the major histocompatibility complex class II I-Ak molecule and to be recognized in this context by two T-cell hybridomas, specific for the parent peptide HEL[52-61]. The data showed that the conformation and also the configuration of the Tyr53 residue influenced both the binding of the peptide to I-Ak and the recognition of the peptide/I-Ak complex by a T-cell receptor.

Side chain

Residue (chemistry)

Cyclic peptide

10.1034/j.1399-3011.2000.00777.x

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Citations (12)

Mechanism of Measles Virus–Induced Suppression of Inflammatory Immune Responses

Immunity (2001)

Julien C. Marie Jeanne Kehren Marie-Claude Trescol-Biémont Alexey Evlashev Hélène Valentin

Immunosuppression

Nucleoprotein

10.1016/s1074-7613(01)00090-5

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Citations (140)

FcγR expressed on T-cell hybrids: Specificity, behavior and relationship with Ia antigens

Cellular Immunology (1981)

Jean‐Luc Teillaud Chantal Rabourdin‐Combe M Stanislawski Catheriné Sautès-Fridman Wolf H. Fridman

10.1016/0008-8749(81)90014-9

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Citations (9)

Differential permissivity to measles virus infection of human and CD46-transgenic murine lymphocytes

Journal of General Virology (2001)

Alexey Evlashev Hélène Valentin Pierre Rivailler Olga Azocar Chantal Rabourdin‐Combe

Analysis of measles virus (MV) pathogenesis requires the development of an adequate small animal model of MV infection. In this study, permissivity to MV infection was compared in human and transgenic murine T lymphocytes, expressing different levels of the human MV receptor, CD46. Whereas MV binding and entry correlated with CD46 expression, higher levels of MV replication were always observed in human T lymphocytes. This suggests the existence of intracellular factors, acting posterior to virus entry, that could limit MV replication in murine lymphocytes and should be considered when creating new animal models of MV infection.

Pathogenesis

10.1099/0022-1317-82-9-2125

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Citations (14)

System-Level Comparison of Protein−Protein Interactions between Viruses and the Human Type I Interferon System Network

Journal of Proteome Research (2010)

Vincent Navratil Benoı̂t de Chassey Laurène Meyniel‐Schicklin Fabrine Pradezynski Patrice André

Innate immunity has evolved complex molecular pathways to protect organisms from viral infections. One pivotal line of cellular defense is the induction of the antiviral effect of interferon. To circumvent this primary response and achieve their own replication, viruses have developed complex molecular strategies. Here, we provide a systems-level study of the human type I interferon system subversion by the viral proteome, by reconstructing the underlying protein−protein interaction network. At this network level, viruses establish a massive and a gradual attack, from receptors to transcription factors, by interacting preferentially with highly connected and central proteins as well as interferon-induced proteins. We also demonstrate that viruses significantly target 22% of the proteins directly interacting with the type I interferon system network, suggesting the relevance of our network-based method to identify new candidates involved in the regulation of the antiviral response. Finally, based on the comparative analysis of interactome profiles across four viral families, we provide evidence of common and differential targeting strategies.

Interactome

Proteome

Interaction network

Interferon type I

10.1021/pr100326j

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Citations (33)

Immature dendritic cell transdifferentiation into osteoclasts: a novel pathway sustained by the rheumatoid arthritis microenvironment

Blood (2004)

Aymeric Rivollier M. Mazzorana Jacques Tébib Muriel Piperno Tarik Aitsiselmi

Transdifferentiation

Proinflammatory cytokine

Monocyte

10.1182/blood-2004-01-0041

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Citations (303)

Measles Virus Infection Induces Terminal Differentiation of Human Thymic Epithelial Cells

Journal of Virology (1999)

Hélène Valentin Olga Azocar Branka Horvat Rejane Williems R. Garrone

ABSTRACT Measles virus infection induces a profound immunosuppression that may lead to serious secondary infections and mortality. In this report, we show that the human cortical thymic epithelial cell line is highly susceptible to measles virus infection in vitro, resulting in infectious viral particle production and syncytium formation. Measles virus inhibits thymic epithelial cell growth and induces an arrest in the G 0 /G 1 phases of the cell cycle. Moreover, we show that measles virus induces a progressive thymic epithelial cell differentiation process: attached measles virus-infected epithelial cells correspond to an intermediate state of differentiation while floating cells, recovered from cell culture supernatants, are fully differentiated. Measles virus-induced thymic epithelial cell differentiation is characterized by morphological and phenotypic changes. Measles virus-infected attached cells present fusiform and stellate shapes followed by a loss of cell-cell contacts and a shift from low- to high-molecular-weight keratin expression. Measles virus infection induces thymic epithelial cell apoptosis in terminally differentiated cells, revealed by the condensation and degradation of DNA in measles virus-infected floating thymic epithelial cells. Because thymic epithelial cells are required for the generation of immunocompetent T lymphocytes, our results suggest that measles virus-induced terminal differentiation of thymic epithelial cells may contribute to immunosuppression, particularly in children, in whom the thymic microenvironment is of critical importance for the development and maturation of a functional immune system.

Syncytium

10.1128/jvi.73.3.2212-2221.1999

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Citations (47)