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12 results on '"Rey, Felix"'

1. Common Features of Enveloped Viruses and Implications for Immunogen Design for Next-Generation Vaccines.

Author

Rey FA and Lok SM

Subjects
Animals, Drug Design, Host-Pathogen Interactions immunology, Humans, Viral Envelope Proteins immunology, Viral Fusion Proteins immunology, Viral Fusion Proteins metabolism, Virus Diseases virology, Viruses metabolism, Vaccines, Synthetic immunology, Viral Vaccines immunology, Virus Diseases immunology, Viruses immunology
Abstract

Enveloped viruses enter cells by inducing fusion of viral and cellular membranes, a process catalyzed by a specialized membrane-fusion protein expressed on their surface. This review focuses on recent structural studies of viral fusion proteins with an emphasis on their metastable prefusion form and on interactions with neutralizing antibodies. The fusion glycoproteins have been difficult to study because they are present in a labile, metastable form at the surface of infectious virions. Such metastability is a functional requirement, allowing these proteins to refold into a lower energy conformation while transferring the difference in energy to catalyze the membrane fusion reaction. Structural studies have shown that stable immunogens presenting the same antigenic sites as the labile wild-type proteins efficiently elicit potently neutralizing antibodies, providing a framework with which to engineer the antigens for stability, as well as identifying key vulnerability sites that can be used in next-generation subunit vaccine design., (Copyright © 2018 Elsevier Inc. All rights reserved.)

Published
2018
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2. Virus structure and function.

Author

Marcotrigiano J and Rey FA

Subjects
Viral Proteins chemistry, Viral Proteins metabolism, Virus Physiological Phenomena, Viruses pathogenicity, Viruses ultrastructure
Published
2013
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3. SnapShot: Viral and eukaryotic protein fusogens.

Author

Igonet S and Rey FA

Subjects
Animals, Cytoplasmic Vesicles metabolism, Humans, SNARE Proteins chemistry, SNARE Proteins metabolism, Viral Fusion Proteins chemistry, Viruses chemistry, Eukaryota virology, Membrane Fusion, Viral Fusion Proteins metabolism, Viruses metabolism
Published
2012
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9. A LIVE AND ATTENUATED FLAVIVIRUS COMPRISING A MUTATED M PROTEIN FIELD OF THE INVENTION 5 BACKGROUND OF THE INVENTION

Author

Pardigon, Nathalie, Rey, Felix, Basset, Justine, Environnement et Risques infectieux - Environment and Infectious Risks (ERI), Institut Pasteur [Paris], Virologie Structurale - Structural Virology, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Cellule Pasteur, Université Paris Diderot - Paris 7 (UPD7)-PRES Sorbonne Paris Cité, Institut Pasteur [Paris] (IP), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
viruses, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, virus diseases, complex mixtures, nervous system diseases
Abstract

The application relates to the attenuation of flaviviruses, such as West Nile Virus (WNV). The application notably provides a live and attenuated flavivirus, such as a WNV, comprising a mutated M protein. Said mutated M protein comprises or consists of a sequence, wherein the amino acids at position 36 in the ectodomain and position 43 in the transmembrane 10 domain 1 in said sequence are mutated. The application also provides additional embodiments deriving from said live and attenuated flavivirus, such as a WNV, such as nucleic acids, cDNA clones, immunogenic compositions as well as uses and methods.

Published
2019

10. Structural insights into the neutralization mechanism of a higher primate antibody against dengue virus

Author

Cockburn, Joseph, Navarro Sanchez, M Erika, Goncalvez, Ana, Zaitseva, Elena, Stura, Enrico, Kikuti, Carlos, Duquerroy, Stéphane, Dussart, Philippe, Chernomordik, Leonid, Lai, Ching-Juh, Rey, Felix, Virologie Structurale, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), National Institutes of Health [Bethesda] (NIH), Laboratoire de Toxinologie Moléculaire et Biotechnologies (LTMB), Service d'Ingénierie Moléculaire pour la Santé (ex SIMOPRO) (SIMoS), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Pasteur de la Guyane, Réseau International des Instituts Pasteur (RIIP), This work was supported by a PDVI grant to FAR, the Intramural Research Program of the National Institute of Allergy and Infectious Diseases to CJL, the Intramural Research Program of the Eunice Kennedy Shriver National Institute of Child Health and Human Development and a National Institutes of Health Intramural Biodefense Research grant (both to LVC). JJBC was supported by an EMBO long-term fellowship (ALTF-194-2005) and a Marie Curie Intra-European Fellowship (EIF-25456-DENLIG). FAR also acknowledges support from Merck-Serono and from the ANR grant ‘DENTRY’., ANR-05-MIIM-0012,DENtry,Entrée des flavivirus dans les cellules cibles : identification et analyse structurale de récepteurs du virus de la Dengue et caractérisation des voies d'entrée virale - Elargissement des études structurales à d'autres virus enveloppés de classe II(2005), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Primates, MESH: Sequence Homology, Amino Acid, viruses, Molecular Sequence Data, MESH: Amino Acid Sequence, Antibodies, Viral, MESH: Dengue Virus, Article, Viral Proteins, Neutralization Tests, antibody, Animals, MESH: Animals, Amino Acid Sequence, structure, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, MESH: Neutralization Tests, Dengue Virus, dengue, MESH: Viral Proteins, MESH: Primates, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Antibodies, Viral, MESH: Models, Molecular
Abstract

International audience; The four serotypes of dengue virus (DENV-1 to-4) cause the most important emerging viral disease. Protein E, the principal viral envelope glycoprotein, mediates fusion of the viral and endosomal membranes during virus entry and is the target of neutralizing antibodies. However, the epitopes of strongly neutralizing human antibodies have not been described despite their importance to vaccine development. The chimpanzee Mab 5H2 potently neutralizes DENV-4 by binding to domain I of E. The crystal structure of Fab 5H2 bound to E from DENV-4 shows that antibody binding prevents formation of the fusogenic hairpin conformation of E, which together with in-vitro assays, demonstrates that 5H2 neutralizes by blocking membrane fusion in the endosome. Furthermore, we show that human sera from patients recovering from DENV-4 infection contain antibodies that bind to the 5H2 epitope region on domain I. This study, thus, provides new information and tools for effective vaccine design to prevent dengue disease.

Published
2011
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11. Les relations structurales entre birnavirus et autres virus icosaédriques à ARN

Author

Coulibaly, Fasseli, Chevalier, Christophe, Galloux, Marie, da Costa, Bruno, Lepault, Jean, Delmas, Bernard, Rey, Felix, Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA), Unité de recherche Virologie et Immunologie Moléculaires (VIM (UR 0892)), Virologie moléculaire et structurale (VMS), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), and ProdInra, Migration

Subjects
[SDV] Life Sciences [q-bio], viruses, [SDV]Life Sciences [q-bio]
Abstract

National audience; Les particules des virus à ARN double brin (ARNdb) sont compétentes pour la transcription et doivent traverser une membrane cellulaire pour fonctionner dans le cytoplasme de la cellule cible. Parmi ces virus, les birnavirus sont singuliers car ils possèdent une simple capside icosaédrique de triangulation T = 13 et ne contiennent pas la capside interne caractéristique observée dans la plupart de ces virus. Nous avons récemment élucidé la structure de sous-particules virales ainsi que de particules virales complètes d’un birnavirus aviaire [1]. Nos résultats révèlent des relations structurales inattendues entre virus icosaédriques et nous permettent de proposer un lien phylogénétique entre certains virus à ARNdb et des virus à ARN de polarité positive.

Published
2006

12. Class II enveloped viruses.

Author

Vaney, Marie-Christine and Rey, Felix A.

Subjects
*VIRUSES, *VIRAL genomes, *CELLS, *LIPIDS, *RNA viruses, *VIRION, *PROTEIN precursors, *GLYCOPROTEINS, *BUNYAVIRUSES
Abstract

Summary A number of viruses transport their genomic material from cell to cell enclosed within a lipid bilayer that is in turn encased within a symmetric protein shell. This review focuses in a group of RNA viruses that have this type of virions. This group includes several of important human pathogenic viruses, such as the hepatitis C virus, dengue virus, chikungunya virus, rubella virus and the bunyaviruses. The best studied are the flaviviruses and the alphaviruses, which have a β-sheet rich class II viral fusion protein used for entry into susceptible cells. We extend here the class II concept to encompass symmetric viruses in which the envelope proteins are derived from a precursor polyprotein containing two transmembrane glycoproteins arranged in tandem. The first glycoprotein acts as chaperone for the folding of the second one, which carries the membrane fusion function. Since the bunyaviruses, included here, are very similar to the class I arenaviruses in other respects, this analysis highlights the patchwork nature of the various viral functional modules acting at different stages of the virus cycle, which appear assembled from genes of different origins. [ABSTRACT FROM AUTHOR]

Published
2011
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