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154. The Role of Heterotypic DENV-specific CD8+T Lymphocytes in an Immunocompetent Mouse Model of Secondary Dengue Virus Infection

Author

Talarico, Laura B., primary, Batalle, Juan P., additional, Byrne, Alana B., additional, Brahamian, Jorge M., additional, Ferretti, Adrián, additional, García, Ayelén G., additional, Mauri, Aldana, additional, Simonetto, Carla, additional, Hijano, Diego R., additional, Lawrence, Andrea, additional, Acosta, Patricio L., additional, Caballero, Mauricio T., additional, Paredes Rojas, Yésica, additional, Ibañez, Lorena I., additional, Melendi, Guillermina A., additional, Rey, Félix A., additional, Damonte, Elsa B., additional, Harris, Eva, additional, and Polack, Fernando P., additional

Published
2017
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156. Structural Snapshots of Eff-1 Mediated Membrane Fusion

Author

Dellarole, Mariano, primary, Meola, Annalisa, additional, Pehau-Arnaudet, Gérard, additional, Bontems, François, additional, Borgnia, Mario J., additional, Krey, Thomas, additional, Volkmann, Niels, additional, Hanein, Dorit, additional, and Rey, Félix A., additional

Published
2017
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157. A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion

Author

dI&I I&I-1, Guardado-Calvo, P, Atkovska, K, Jeffers, S A, Grau, N, Backovic, M, Pérez-Vargas, J, de Boer, S M, Tortorici, M Alejandra, Pehau-Arnaudet, G., Lepault, J., England, P., Rottier, P J, Bosch, B J, Hub, J S, Rey, Félix A, dI&I I&I-1, Guardado-Calvo, P, Atkovska, K, Jeffers, S A, Grau, N, Backovic, M, Pérez-Vargas, J, de Boer, S M, Tortorici, M Alejandra, Pehau-Arnaudet, G., Lepault, J., England, P., Rottier, P J, Bosch, B J, Hub, J S, and Rey, Félix A

Published
2017

158. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer

Author

Walls, Alexandra C, Tortorici, M Alejandra, Bosch, Berend-Jan, Frenz, Brandon, Rottier, Peter J M, DiMaio, Frank, Rey, Félix A, Veesler, David, Walls, Alexandra C, Tortorici, M Alejandra, Bosch, Berend-Jan, Frenz, Brandon, Rottier, Peter J M, DiMaio, Frank, Rey, Félix A, and Veesler, David

Abstract

The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions. S also contains the principal antigenic determinants and is the target of neutralizing antibodies. Here we present the structure of a mouse coronavirus S trimer ectodomain determined at 4.0 Å resolution by single particle cryo-electron microscopy. It reveals the metastable pre-fusion architecture of S and highlights key interactions stabilizing it. The structure shares a common core with paramyxovirus F proteins, implicating mechanistic similarities and an evolutionary connection between these viral fusion proteins. The accessibility of the highly conserved fusion peptide at the periphery of the trimer indicates potential vaccinology strategies to elicit broadly neutralizing antibodies against coronaviruses. Finally, comparison with crystal structures of human coronavirus S domains allows rationalization of the molecular basis for species specificity based on the use of spatially contiguous but distinct domains.

Published
2016

159. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Author

dI&I I&I-1, Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., LS Virologie, Infection & Immunity, Walls, Alexandra C, Tortorici, M Alejandra, Frenz, Brandon, Snijder, Joost, Li, Wentao, Rey, Félix A, DiMaio, Frank, Bosch, Berend-Jan, Veesler, David, dI&I I&I-1, Biomolecular Mass Spectrometry and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., LS Virologie, Infection & Immunity, Walls, Alexandra C, Tortorici, M Alejandra, Frenz, Brandon, Snijder, Joost, Li, Wentao, Rey, Félix A, DiMaio, Frank, Bosch, Berend-Jan, and Veesler, David

Published
2016

160. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer

Author

LS Virologie, dI&I I&I-1, Walls, Alexandra C, Tortorici, M Alejandra, Bosch, Berend-Jan, Frenz, Brandon, Rottier, Peter J M, DiMaio, Frank, Rey, Félix A, Veesler, David, LS Virologie, dI&I I&I-1, Walls, Alexandra C, Tortorici, M Alejandra, Bosch, Berend-Jan, Frenz, Brandon, Rottier, Peter J M, DiMaio, Frank, Rey, Félix A, and Veesler, David

Published
2016

161. An Open Receptor-Binding Cavity of Hemagglutinin-Esterase-Fusion Glycoprotein from Newly-Identified Influenza D Virus: Basis for Its Broad Cell Tropism.

Author

Song, Hao, Rey, Félix A1, Song, Hao, Qi, Jianxun, Khedri, Zahra, Diaz, Sandra, Yu, Hai, Chen, Xi, Varki, Ajit, Shi, Yi, Gao, George F, Song, Hao, Rey, Félix A1, Song, Hao, Qi, Jianxun, Khedri, Zahra, Diaz, Sandra, Yu, Hai, Chen, Xi, Varki, Ajit, Shi, Yi, and Gao, George F

Abstract

Influenza viruses cause seasonal flu each year and pandemics or epidemic sporadically, posing a major threat to public health. Recently, a new influenza D virus (IDV) was isolated from pigs and cattle. Here, we reveal that the IDV utilizes 9-O-acetylated sialic acids as its receptor for virus entry. Then, we determined the crystal structures of hemagglutinin-esterase-fusion glycoprotein (HEF) of IDV both in its free form and in complex with the receptor and enzymatic substrate analogs. The IDV HEF shows an extremely similar structural fold as the human-infecting influenza C virus (ICV) HEF. However, IDV HEF has an open receptor-binding cavity to accommodate diverse extended glycan moieties. This structural difference provides an explanation for the phenomenon that the IDV has a broad cell tropism. As IDV HEF is structurally and functionally similar to ICV HEF, our findings highlight the potential threat of the virus to public health.

Published
2016

162. Mechanistic Insight into Bunyavirus-Induced Membrane Fusion from Structure-Function Analyses of the Hantavirus Envelope Glycoprotein Gc

Author

Guardado-Calvo, Pablo, primary, Bignon, Eduardo A., additional, Stettner, Eva, additional, Jeffers, Scott Allen, additional, Pérez-Vargas, Jimena, additional, Pehau-Arnaudet, Gerard, additional, Tortorici, M. Alejandra, additional, Jestin, Jean-Luc, additional, England, Patrick, additional, Tischler, Nicole D., additional, and Rey, Félix A., additional

Published
2016
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163. Erratum: Structural basis of potent Zika–dengue virus antibody cross-neutralization

Author

Barba-Spaeth, Giovanna, primary, Dejnirattisai, Wanwisa, additional, Rouvinski, Alexander, additional, Vaney, Marie-Christine, additional, Medits, Iris, additional, Sharma, Arvind, additional, Simon-Lorière, Etienne, additional, Sakuntabhai, Anavaj, additional, Cao-Lormeau, Van-Mai, additional, Haouz, Ahmed, additional, England, Patrick, additional, Stiasny, Karin, additional, Mongkolsapaya, Juthathip, additional, Heinz, Franz X., additional, Screaton, Gavin R., additional, and Rey, Félix A., additional

Published
2016
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165. Marburg Virus Structure Revealed in Detail

Author

Bharat, Tanmay A. M., Riches, James D., Kolesnikova, Larissa, Welsch, Sonja, Krähling, Verena, Davey, Norman, Rey, Félix A., Parsy, Marie-Laure, Becker, Stephan, and Briggs, John A. G.

Subjects
Macromolecular Assemblies, Electron Microscope Tomography, viruses, 060506 Virology, cryo electron tomography, medicine.disease_cause, Molecular Cell Biology, Macromolecular Structure Analysis, Viral Regulatory and Accessory Proteins, Biology (General), ebola virus, Virus Release, biology, General Neuroscience, Cell biology, Host-Pathogen Interaction, Vesicular stomatitis virus, Synopsis, RNA, Viral, Cryo-electron tomography, Membranes and Sorting, General Agricultural and Biological Sciences, Research Article, Protein Structure, QH301-705.5, Biophysics, Viral Structure, Microbiology, General Biochemistry, Genetics and Molecular Biology, Cell Line, Marburg virus, Viral Proteins, VP40, Virology, Viruslike Particles, medicine, Humans, Nucleocapsid, marburg virus, Biology, Viral matrix protein, Ebola virus, General Immunology and Microbiology, Virus Assembly, Cryoelectron Microscopy, Host Cells, RNA, Computational Biology, biology.organism_classification, Marburgvirus, Nucleoprotein, HEK293 Cells, Nucleoproteins, Rabies virus, Ultrastructure, 060112 Structural Biology (incl. Macromolecular Modelling), Viral Transmission and Infection
Abstract

Ultrastructural analysis of a filovirus assembling within infected eukaryotic cells reveals differences in structure and assembly mechanisms between related RNA viruses., Several major human pathogens, including the filoviruses, paramyxoviruses, and rhabdoviruses, package their single-stranded RNA genomes within helical nucleocapsids, which bud through the plasma membrane of the infected cell to release enveloped virions. The virions are often heterogeneous in shape, which makes it difficult to study their structure and assembly mechanisms. We have applied cryo-electron tomography and sub-tomogram averaging methods to derive structures of Marburg virus, a highly pathogenic filovirus, both after release and during assembly within infected cells. The data demonstrate the potential of cryo-electron tomography methods to derive detailed structural information for intermediate steps in biological pathways within intact cells. We describe the location and arrangement of the viral proteins within the virion. We show that the N-terminal domain of the nucleoprotein contains the minimal assembly determinants for a helical nucleocapsid with variable number of proteins per turn. Lobes protruding from alternate interfaces between each nucleoprotein are formed by the C-terminal domain of the nucleoprotein, together with viral proteins VP24 and VP35. Each nucleoprotein packages six RNA bases. The nucleocapsid interacts in an unusual, flexible “Velcro-like” manner with the viral matrix protein VP40. Determination of the structures of assembly intermediates showed that the nucleocapsid has a defined orientation during transport and budding. Together the data show striking architectural homology between the nucleocapsid helix of rhabdoviruses and filoviruses, but unexpected, fundamental differences in the mechanisms by which the nucleocapsids are then assembled together with matrix proteins and initiate membrane envelopment to release infectious virions, suggesting that the viruses have evolved different solutions to these conserved assembly steps., Author Summary Marburg virus and Ebola virus cause severe hemorrhagic fever in humans and non human primates. They are members of the family of Filoviridae, and part of the order Mononegavirales, which includes other important human pathogens: rabies virus, respiratory syncytial virus, and measles virus. All of these viruses contain a single-stranded RNA genome enclosed within a helical protein assembly called the nucleocapsid. In this study, we used electron microscopy to image individual Marburg virus particles, allowing us to determine the architecture of the nucleocapsid and the positions of the viral proteins. We found that the nucleocapsid structure contained a “barbed” and a “pointed” end, and was similar to that of the related family of bullet-shaped Rhabdoviridae, which includes rabies virus. When we generated 3-D images of virus particles frozen in the act of assembling and budding from infected cells, however, we found that despite their structural similarities, Marburg virus particles are released from infected cells with the pointed end of the nucleocapsid facing out, whereas rabies virus is released with its barbed end facing out, suggesting different budding mechanisms. This study illustrates not only how electron microscopy of frozen samples can resolve structural information in vivo, but it provides knowledge of the structure of a filovirus and its assembly pathway, generated by direct 3-D imaging of infected cells, revealing similarities and differences in the assembly and budding mechanisms of members of Mononegavirales.

Published
2011

166. Class II enveloped viruses

Author

Vaney, Marie-Christine, Rey, Félix A., Virologie Structurale, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Viral Matrix Proteins, Protein Folding, Viral Envelope Proteins, viruses, [CHIM.CRIS]Chemical Sciences/Cristallography, Animals, Humans, RNA Viruses, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Virus Internalization, Molecular Chaperones
Abstract

International audience; 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.

Published
2011
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167. Virology: One protein, many functions

Author

Rey, Félix A., Virologie Structurale, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)

Subjects
viruses, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Abstract

International audience; The Lassa virus nucleoprotein coats the viral genome to make a template for RNA synthesis. A study shows that it also binds the 'cap' structure of cellular messenger RNAs and directs immune evasion using a novel mechanism.

Published
2010
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168. A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of Human Respiratory Syncytial Virus

Author

Ouizougun-Oubari, Mohamed, primary, Pereira, Nelson, additional, Tarus, Bogdan, additional, Galloux, Marie, additional, Lassoued, Safa, additional, Fix, Jenna, additional, Tortorici, M. Alejandra, additional, Hoos, Sylviane, additional, Baron, Bruno, additional, England, Patrick, additional, Desmaële, Didier, additional, Couvreur, Patrick, additional, Bontems, François, additional, Rey, Félix A., additional, Eléouët, Jean-François, additional, Sizun, Christina, additional, Slama-Schwok, Anny, additional, and Duquerroy, Stéphane, additional

Published
2015
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170. CD209+ Macrophages Resist Dengue Virus

Author

Kwan, Wing-Hong, Navarro-Sanchez, Erika, Dumortier, Hélène, Decossas, Marion, Vachon, Hortense, dos Santos, Flavia Barreto, Fridman, Hervé W, Rey, Félix A., Harris, Eva, Desprès, Philippe, Mueller, Christopher G, Pansiot, Sylvie, Immunologie et chimie thérapeutiques (ICT), Cancéropôle du Grand Est-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S 872)), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Interactions Moléculaires Flavivirus-Hôtes, Institut Pasteur [Paris] (IP), Virologie Structurale, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Division of Infectious Diseases, University of California (UC), and This work was supported by INSERM, CNRS, the Fondation de la Recherche Me´ dicale, the Agence Nationale de Recherche Microbiologie Immunologie Maladies Emergentes (contract ARBO-CELLGUARD), the Pediatric Dengue Vaccine Initiative (PDVI), and the European Commission (INCO-DEV, contract DENFRAME No. 51711). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

Subjects
[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, viruses, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases
Abstract

International audience; BACKGROUND: An important question in dengue pathogenesis is the identity of immune cells involved in the control of dengue virus infection at the site of the mosquito bite. There is evidence that infection of immature myeloid dendritic cells plays a crucial role in dengue pathogenesis and that the interaction of the viral envelope E glycoprotein with CD209/DC-SIGN is a key element for their productive infection. Dermal macrophages express CD209, yet little is known about their role in dengue virus infection. METHODS AND FINDINGS: Here, we showed that dermal macrophages bound recombinant envelope E glycoprotein fused to green fluorescent protein. Because dermal macrophages stain for IL-10 in situ, we generated dermal-type macrophages from monocytes in the presence of IL-10 to study their infection by dengue virus. The macrophages were able to internalize the virus, but progeny virus production was undetectable in the infected cells. In addition, no IFN-alpha was produced in response to the virus. The inability of dengue virus to grow in the macrophages was attributable to accumulation of internalized virus particles into poorly-acidified phagosomes. CONCLUSIONS: Aborting infection by viral sequestration in early phagosomes would present a novel means to curb infection of enveloped virus and may constitute a prime defense system to prevent dengue virus spread shortly after the bite of the infected mosquito.

Published
2008
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171. Virology: holed up in a natural crystal

Author

Rey, Félix A., Virologie Structurale, Institut Pasteur [Paris], and Institut Pasteur [Paris] (IP)

Subjects
MESH: Insects, MESH: Protein Conformation, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, MESH: Inclusion Bodies, Viral, MESH: Animals, MESH: Crystallography, X-Ray, MESH: Viral Proteins, MESH: Models, Molecular, MESH: Nucleopolyhedrovirus, MESH: Crystallization
Published
2007
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172. Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein

Author

Duquerroy, Stéphane, Vigouroux, Armelle, Rottier, Peter J M, Rey, Félix A, Bosch, Berend Jan, LS Virologie, and LS Virologie

Subjects
Models, Molecular, Protein Conformation, viruses, Glutamine, Molecular Sequence Data, Static Electricity, Coronacrisis-Taverne, Spike protein, Biology, medicine.disease_cause, Antiparallel (biochemistry), Membrane Fusion, Article, Protein structure, Viral Envelope Proteins, Models, Virology, medicine, Asparagine, Amino Acid Sequence, Coiled coil, Coronavirus, SARS, Ions, Membrane Glycoproteins, Membrane fusion protein, Structure, Molecular, SARS Virus, Spike Glycoprotein, Heptad repeat, Severe acute respiratory syndrome-related coronavirus, Biochemistry, Ectodomain, Asparagine zipper, Spike Glycoprotein, Coronavirus, Class I fusion protein, Biophysics, Thermodynamics, Salts, Protein Binding
Abstract

The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 Å) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding “zippers” that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 α-helix.

Published
2005

173. Electron tomography of HIV-1 infection in gut-associated lymphoid tissue.

Author

Ladinsky, Mark S, Rey, Félix A1, Ladinsky, Mark S, Kieffer, Collin, Olson, Gregory, Deruaz, Maud, Vrbanac, Vladimir, Tager, Andrew M, Kwon, Douglas S, Bjorkman, Pamela J, Ladinsky, Mark S, Rey, Félix A1, Ladinsky, Mark S, Kieffer, Collin, Olson, Gregory, Deruaz, Maud, Vrbanac, Vladimir, Tager, Andrew M, Kwon, Douglas S, and Bjorkman, Pamela J

Abstract

Critical aspects of HIV-1 infection occur in mucosal tissues, particularly in the gut, which contains large numbers of HIV-1 target cells that are depleted early in infection. We used electron tomography (ET) to image HIV-1 in gut-associated lymphoid tissue (GALT) of HIV-1-infected humanized mice, the first three-dimensional ultrastructural examination of HIV-1 infection in vivo. Human immune cells were successfully engrafted in the mice, and following infection with HIV-1, human T cells were reduced in GALT. Virions were found by ET at all stages of egress, including budding immature virions and free mature and immature viruses. Immuno-electron microscopy verified the virions were HIV-1 and showed CD4 sequestration in the endoplasmic reticulum of infected cells. Observation of HIV-1 in infected GALT tissue revealed that most HIV-1-infected cells, identified by immunolabeling and/or the presence of budding virions, were localized to intestinal crypts with pools of free virions concentrated in spaces between cells. Fewer infected cells were found in mucosal regions and the lamina propria. The preservation quality of reconstructed tissue volumes allowed details of budding virions, including structures interpreted as host-encoded scission machinery, to be resolved. Although HIV-1 virions released from infected cultured cells have been described as exclusively mature, we found pools of both immature and mature free virions within infected tissue. The pools could be classified as containing either mostly mature or mostly immature particles, and analyses of their proximities to the cell of origin supported a model of semi-synchronous waves of virion release. In addition to HIV-1 transmission by pools of free virus, we found evidence of transmission via virological synapses. Three-dimensional EM imaging of an active infection within tissue revealed important differences between cultured cell and tissue infection models and furthered the ultrastructural understanding of HIV

Published
2014

175. A nicotinic hypothesis for Covid-19 with preventive and therapeutic implications

Author

Changeux, Jean-Pierre, Amoura, Zahir, Rey, Felix A., and Miyara, Makoto

Subjects
Covid-19, smoking, nicotinic receptors, clinical trials of nicotine patches, Biology (General), QH301-705.5
Abstract

SARS-CoV-2 epidemics raises a considerable issue of public health at the planetary scale. There is a pressing urgency to find treatments based upon currently available scientific knowledge. Therefore, we tentatively propose a hypothesis which hopefully might ultimately help save lives. Based on the current scientific literature and on new epidemiological data which reveal that current smoking status appears to be a protective factor against the infection by SARS-CoV-2 [1], we hypothesize that the nicotinic acetylcholine receptor (nAChR) plays a key role in the pathophysiology of Covid-19 infection and might represent a target for the prevention and control of Covid-19 infection.

Published
2020
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182. Secreted dengue virus nonstructural protein NS1 is an atypical barrel-shaped high-density lipoprotein

Author

Gutsche, Irina, primary, Coulibaly, Fasséli, additional, Voss, James E., additional, Salmon, Jérôme, additional, d'Alayer, Jacques, additional, Ermonval, Myriam, additional, Larquet, Eric, additional, Charneau, Pierre, additional, Krey, Thomas, additional, Mégret, Françoise, additional, Guittet, Eric, additional, Rey, Félix A., additional, and Flamand, Marie, additional

Published
2011
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184. The Disulfide Bonds in Glycoprotein E2 of Hepatitis C Virus Reveal the Tertiary Organization of the Molecule

Author

Krey, Thomas, primary, d'Alayer, Jacques, additional, Kikuti, Carlos M., additional, Saulnier, Aure, additional, Damier-Piolle, Laurence, additional, Petitpas, Isabelle, additional, Johansson, Daniel X., additional, Tawar, Rajiv G., additional, Baron, Bruno, additional, Robert, Bruno, additional, England, Patrick, additional, Persson, Mats A. A., additional, Martin, Annette, additional, and Rey, Félix A., additional

Published
2010
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188. Dermal-Type Macrophages Expressing CD209/DC-SIGN Show Inherent Resistance to Dengue Virus Growth

Author

Kwan, Wing-Hong, primary, Navarro-Sanchez, Erika, additional, Dumortier, Hélène, additional, Decossas, Marion, additional, Vachon, Hortense, additional, Santos, Flavia Barreto dos, additional, Fridman, Hervé W., additional, Rey, Félix A., additional, Harris, Eva, additional, Despres, Philippe, additional, and Mueller, Christopher G., additional

Published
2008
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190. Recognition determinants of broadly neutralizing human antibodies against dengue viruses.

Author

Rouvinski, Alexander, Guardado-Calvo, Pablo, Barba-Spaeth, Giovanna, Duquerroy, Stéphane, Vaney, Marie-Christine, Kikuti, Carlos M., Navarro Sanchez, M. Erika, Dejnirattisai, Wanwisa, Wongwiwat, Wiyada, Haouz, Ahmed, Girard-Blanc, Christine, Petres, Stéphane, Shepard, William E., Desprès, Philippe, Arenzana-Seisdedos, Fernando, Dussart, Philippe, Mongkolsapaya, Juthathip, Screaton, Gavin R., and Rey, Félix A.

Subjects
DENGUE, FLAVIVIRAL diseases, SEROTYPES, GLYCANS, GLYCOPROTEINS
Abstract

Dengue disease is caused by four different flavivirus serotypes, which infect 390 million people yearly with 25% symptomatic cases and for which no licensed vaccine is available. Recent phase III vaccine trials showed partial protection, and in particular no protection for dengue virus serotype 2 (refs 3, 4). Structural studies so far have characterized only epitopes recognized by serotype-specific human antibodies. We recently isolated human antibodies potently neutralizing all four dengue virus serotypes. Here we describe the X-ray structures of four of these broadly neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, revealing that the recognition determinants are at a serotype-invariant site at the E-dimer interface, including the exposed main chain of the E fusion loop and the two conserved glycan chains. This 'E-dimer-dependent epitope' is also the binding site for the viral glycoprotein prM during virus maturation in the secretory pathway of the infected cell, explaining its conservation across serotypes and highlighting an Achilles' heel of the virus with respect to antibody neutralization. These findings will be instrumental for devising novel immunogens to protect simultaneously against all four serotypes of dengue virus. [ABSTRACT FROM AUTHOR]

Published
2015
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192. Genome Microevolution of Chikungunya Viruses Causing the Indian Ocean Outbreak

Author

Schuffenecker, Isabelle, primary, Iteman, Isabelle, additional, Michault, Alain, additional, Murri, Séverine, additional, Frangeul, Lionel, additional, Vaney, Marie-Christine, additional, Lavenir, Rachel, additional, Pardigon, Nathalie, additional, Reynes, Jean-Marc, additional, Pettinelli, François, additional, Biscornet, Leon, additional, Diancourt, Laure, additional, Michel, Stéphanie, additional, Duquerroy, Stéphane, additional, Guigon, Ghislaine, additional, Frenkiel, Marie-Pascale, additional, Bréhin, Anne-Claire, additional, Cubito, Nadège, additional, Desprès, Philippe, additional, Kunst, Frank, additional, Rey, Félix A, additional, Zeller, Hervé, additional, and Brisse, Sylvain, additional

Published
2006
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197. Structure, function, and evolution of the Orthobunyavirusmembrane fusion glycoprotein

Author

Hellert, Jan, Aebischer, Andrea, Haouz, Ahmed, Guardado-Calvo, Pablo, Reiche, Sven, Beer, Martin, and Rey, Félix A.

Abstract

La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirusgenus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc (∼1,000 residues), has a variable N-terminal half (GcS) targeted by the patients’ antibody response and a conserved C-terminal moiety (GcF) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus GcF, revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the GcS-GcFjunction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines.

Published
2023
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199. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Author

Walls, Alexandra C, Tortorici, M Alejandra, Frenz, Brandon, Snijder, Joost, Li, Wentao, Rey, Félix A, DiMaio, Frank, Bosch, Berend-Jan, and Veesler, David

Abstract

Cryo-EM and mass spectrometry analyses of the spike glycoprotein trimer from coronavirus HcoV-NL63 reveal an extensive glycan shield that covers the protein surface, including an epitope targeted by neutralizing antibodies against several coronaviruses.

Published
2016
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200. Structural basis of potent Zika–dengue virus antibody cross-neutralization

Author

Barba-Spaeth, Giovanna, Dejnirattisai, Wanwisa, Rouvinski, Alexander, Vaney, Marie-Christine, Medits, Iris, Sharma, Arvind, Simon-Lorière, Etienne, Sakuntabhai, Anavaj, Cao-Lormeau, Van-Mai, Haouz, Ahmed, England, Patrick, Stiasny, Karin, Mongkolsapaya, Juthathip, Heinz, Franz X., Screaton, Gavin R., and Rey, Félix A.

Abstract

Zika virus is a member of the Flavivirus genus that had not been associated with severe disease in humans until the recent outbreaks, when it was linked to microcephaly in newborns in Brazil and to Guillain–Barré syndrome in adults in French Polynesia. Zika virus is related to dengue virus, and here we report that a subset of antibodies targeting a conformational epitope isolated from patients with dengue virus also potently neutralize Zika virus. The crystal structure of two of these antibodies in complex with the envelope protein of Zika virus reveals the details of a conserved epitope, which is also the site of interaction of the envelope protein dimer with the precursor membrane (prM) protein during virus maturation. Comparison of the Zika and dengue virus immunocomplexes provides a lead for rational, epitope-focused design of a universal vaccine capable of eliciting potent cross-neutralizing antibodies to protect simultaneously against both Zika and dengue virus infections.

Published
2016
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