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4. Immunogenicity and efficacy of          heterologous ChAdOx1–BNT162b2 vaccination

Author

Pozzetto, Bruno, Legros, Vincent, Djebali, Sophia, Barateau, Véronique, Guibert, Nicolas, Villard, Marine, Peyrot, Loïc, Allatif, Omran, Fassier, Jean-Baptiste, Massardier-Pilonchéry, Amélie, Brengel-Pesce, Karen, Yaugel-Novoa, Melyssa, Denolly, Solène, Boson, Bertrand, Bourlet, Thomas, Bal, Antonin, Valette, Martine, Andrieu, Thibault, Lina, Bruno, Cosset, François-Loïc, Paul, Stéphane, Defrance, Thierry, Marvel, Jacqueline, Walzer, Thierry, and Trouillet-Assant, Sophie

Published
2021
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7. The low-density lipoprotein receptor and apolipoprotein E associated with CCHFV particles mediate CCHFV entry into cells

Author

Ritter, Maureen, primary, Canus, Lola, additional, Gautam, Anupriya, additional, Vallet, Thomas, additional, Zhong, Li, additional, Lalande, Alexandre, additional, Boson, Bertrand, additional, Gandhi, Apoorv, additional, Bodoirat, Sergueï, additional, Burlaud-Gaillard, Julien, additional, Freitas, Natalia, additional, Roingeard, Philippe, additional, Barr, John N., additional, Lotteau, Vincent, additional, Legros, Vincent, additional, Mathieu, Cyrille, additional, Cosset, François-Loïc, additional, and Denolly, Solène, additional

Published
2024
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9. A longitudinal study of SARS-CoV-2-infected patients reveals a high correlation between neutralizing antibodies and COVID-19 severity

Author

Legros, Vincent, Denolly, Solène, Vogrig, Manon, Boson, Bertrand, Siret, Eglantine, Rigaill, Josselin, Pillet, Sylvie, Grattard, Florence, Gonzalo, Sylvie, Verhoeven, Paul, Allatif, Omran, Berthelot, Philippe, Pélissier, Carole, Thiery, Guillaume, Botelho-Nevers, Elisabeth, Millet, Guillaume, Morel, Jérôme, Paul, Stéphane, Walzer, Thierry, Cosset, François-Loïc, Bourlet, Thomas, and Pozzetto, Bruno

Published
2021
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11. Dengue virus NS1 secretion is regulated via importin-subunit β1 controlling expression of the chaperone GRp78 and targeted by the clinical drug ivermectin

Author

Denolly, Solène, primary, Guo, Hongbo, additional, Martens, Miriam, additional, Płaszczyca, Anna, additional, Scaturro, Pietro, additional, Prasad, Vibhu, additional, Kongmanas, Kessiri, additional, Punyadee, Nuntaya, additional, Songjaeng, Adisak, additional, Mairiang, Dumrong, additional, Pichlmair, Andreas, additional, Avirutnan, Panisadee, additional, and Bartenschlager, Ralf, additional

Published
2023
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15. A large-scale serological survey in pets from October 2020 through June 2021 in France shows significantly higher exposure to SARS-CoV-2 in cats

Author

Fritz, Matthieu, primary, Elguero, Eric, additional, Becquart, Pierre, additional, Fonclare, Daphné de Riols de, additional, Garcia, Déborah, additional, Beurlet, Stephanie, additional, Denolly, Solène, additional, Boson, Bertrand, additional, Rosolen, Serge G., additional, Cosset, François-Loïc, additional, Briend-Marchal, Alexandra, additional, Legros, Vincent, additional, and Leroy, Eric M., additional

Published
2022
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18. Report of One-Year Prospective Surveillance of SARS-CoV-2 in Dogs and Cats in France with Various Exposure Risks: Confirmation of a Low Prevalence of Shedding, Detection and Complete Sequencing of an Alpha Variant in a Cat

Author

Krafft, Emilie, primary, Denolly, Solène, additional, Boson, Bertrand, additional, Angelloz-Pessey, Sophie, additional, Levaltier, Sophie, additional, Nesi, Nicolas, additional, Corbet, Sandrine, additional, Leterrier, Bryce, additional, Fritz, Matthieu, additional, Leroy, Eric M., additional, Gouilh, Meriadeg Ar, additional, Cosset, François-Loïc, additional, Kodjo, Angeli, additional, and Legros, Vincent, additional

Published
2021
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19. Immunogenicity and efficacy of heterologous ChadOx1/BNT162b2 vaccination

Author

pozzetto, bruno, primary, legros, vincent, additional, Djebali, Sophia, additional, barateau, véronique, additional, guibert, nicolas, additional, Villard, Marine, additional, Peyrot, Loïc, additional, allatif, omran, additional, fassier, jean-baptise, additional, Massardier-Pilonchéry, Amélie, additional, Brengel-Pesce, Karen, additional, Yaugel-Novoa, Melyssa, additional, Denolly, Solène, additional, boson, bertrand, additional, Bourlet, Thomas, additional, Valette, Martine, additional, Andrieu, Thibault, additional, Lina, Bruno, additional, group, Lyon COVID study, additional, Cosset, François-Loïc, additional, Paul, Stéphane, additional, Defrance, Thierry, additional, Marvel, Jacqueline, additional, Walzer, Thierry, additional, and Trouillet-Assant, Sophie, additional

Published
2021
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20. HCV Interplay with Lipoproteins: Inside or Outside the Cells?

Author

François-Loïc, Cosset, Mialon, Chloé, Boson, Bertrand, Granier, Christelle, Denolly, Solène, Virus enveloppés, vecteurs et immunothérapie – Enveloped viruses, Vectors and Immuno-therapy (EVIR), Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Référent HAL, CIRI

Subjects
hepatitis C virus, Virus Assembly, [SDV]Life Sciences [q-bio], Virion, lcsh:QR1-502, immune escape, virus diseases, Review, Hepacivirus, Virus Internalization, Endoplasmic Reticulum, Lipid Metabolism, Hepatitis C, lcsh:Microbiology, [SDV] Life Sciences [q-bio], lipoproteins, Protein Transport, Host-Pathogen Interactions, Animals, Humans, lipidation, cell entry, Signal Transduction
Abstract

International audience; Hepatitis C virus (HCV) infection is a major public health issue leading to chronic liver diseases. HCV particles are unique owing to their particular lipid composition, namely the incorporation of neutral lipids and apolipoproteins. The mechanism of association between HCV virion components and these lipoproteins factors remains poorly understood as well as its impact in subsequent steps of the viral life cycle, such as entry into cells. It was proposed that the lipoprotein biogenesis pathway is involved in HCV morphogenesis; yet, recent evidence indicated that HCV particles can mature and evolve biochemically in the extracellular medium after egress. In addition, several viral, cellular and blood components have been shown to influence and regulate this specific association. Finally, this specific structure and composition of HCV particles was found to influence entry into cells as well as their stability and sensitivity to neutralizing antibodies. Due to its specific particle composition, studying the association of HCV particles with lipoproteins remains an important goal towards the rational design of a protective vaccine.

Published
2020
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23. High prevalence of SARS-CoV-2 antibodies in pets from COVID-19+ households

Author

Fritz, Matthieu, primary, Rosolen, Béatrice, additional, Krafft, Emilie, additional, Becquart, Pierre, additional, Elguero, Eric, additional, Vratskikh, Oxana, additional, Denolly, Solène, additional, Boson, Bertrand, additional, Vanhomwegen, Jessica, additional, Ar Gouilh, Meriadeg, additional, Kodjo, Angeli, additional, Chirouze, Catherine, additional, Rosolen, Serge, additional, Legros, Vincent, additional, and Leroy, Eric M., additional

Published
2020
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24. The interplays between Crimean-Congo hemorrhagic fever virus (CCHFV) M segment-encoded accessory proteins and structural proteins promote virus assembly and infectivity

Author

Freitas, Natalia, primary, Enguehard, Margot, additional, Denolly, Solène, additional, Levy, Camille, additional, Neveu, Gregory, additional, Lerolle, Solène, additional, Devignot, Stephanie, additional, Weber, Friedemann, additional, Bergeron, Eric, additional, Legros, Vincent, additional, and Cosset, François-Loïc, additional

Published
2020
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25. A longitudinal study of SARS-CoV-2 infected patients shows high correlation between neutralizing antibodies and COVID-19 severity

Author

Legros, Vincent, primary, Denolly, Solène, additional, Vogrig, Manon, additional, Boson, Bertrand, additional, Rigaill, Josselin, additional, Pillet, Sylvie, additional, Grattard, Florence, additional, Gonzalo, Sylvie, additional, Verhoeven, Paul, additional, Allatif, Omran, additional, Berthelot, Philippe, additional, Pélissier, Carole, additional, Thierry, Guillaume, additional, Botelho-Nevers, Elisabeth, additional, Paul, Stéphane, additional, Walzer, Thierry, additional, Cosset, François-Loïc, additional, Bourlet, Thomas, additional, and Pozzetto, Bruno, additional

Published
2020
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28. Detection of SARS‐CoV‐2 in two cats during the second wave of the COVID‐19 pandemic in France.

Author

Fritz, Matthieu, Nesi, Nicolas, Denolly, Solène, Boson, Bertrand, Legros, Vincent, Rosolen, Serge G., Briend‐Marchal, Alexandra, Ar Gouilh, Meriadeg, and Leroy, Eric M.

Subjects
PANDEMICS, COVID-19 pandemic, SARS-CoV-2, CATS, COVID-19, MOLECULAR biology, VITRONECTIN
Abstract

Although there are several reports in the literature of SARS‐CoV‐2 infection in cats, few SARS‐CoV‐2 sequences from infected cats have been published. In this study, SARS‐CoV‐2 infection was evaluated in two cats by clinical observation, molecular biology (qPCR and NGS), and serology (microsphere immunoassay and seroneutralization). Following the observation of symptomatic SARS‐CoV‐2 infection in two cats, infection status was confirmed by RT‐qPCR and, in one cat, serological analysis for antibodies against N‐protein and S‐protein, as well as neutralizing antibodies. Comparative analysis of five SARS‐CoV‐2 sequence fragments obtained from one of the cats showed that this infection was not with one of the three recently emerged variants of SARS‐CoV‐2. This study provides additional information on the clinical, molecular, and serological aspects of SARS‐CoV‐2 infection in cats. This study provides additional information on the clinical, molecular, and serological aspects of SARS‐CoV‐2 infection in cats. [ABSTRACT FROM AUTHOR]

Published
2022
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29. Maturation extracellulaire du virus de l’hépatite C

Author

Chanut, Marion, Granier, Christelle, François-Loïc, Cosset, Denolly, Solène, Sciences, EDP, Children's Hospital, Laboratoire d'aérologie (LAERO), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Observatoire Midi-Pyrénées (OMP), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National d'Études Spatiales [Toulouse] (CNES)-Centre National de la Recherche Scientifique (CNRS)-Météo-France -Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National d'Études Spatiales [Toulouse] (CNES)-Centre National de la Recherche Scientifique (CNRS)-Météo-France -Centre National de la Recherche Scientifique (CNRS), NOAA Earth System Research Laboratory (ESRL), National Oceanic and Atmospheric Administration (NOAA), Virus enveloppés, vecteurs et immunothérapie – Enveloped viruses, Vectors and Immuno-therapy (EVIR), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

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

International audience

Published
2019
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31. Assemblage du VHC : du regroupement des facteurs viraux d'assemblage à l'enveloppement et la lipidation des particules

Author

Denolly, Solène, Virus enveloppés, vecteurs et immunothérapie – Enveloped viruses, Vectors and Immuno-therapy (EVIR), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon, François-Loïc Cosset, Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-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)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)

Subjects
Hepatitis C Virus, viruses, Viroporine, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Viral assembly, Assemblage Viral, Virus de l’Hépatite C, Lipidation
Abstract

Hepatitis C virus (HCV) is detected in the sera of infected patients as lipidated infectious particles of very-low density. HCV is an enveloped virus whose assembly of viral particles occurs at the endoplasmic reticulum membrane following sequential cleavage of its polyprotein and its maturation as structural and non-structural viral proteins. In this work, we aimed at better understanding the mechanisms of assembly, envelopment and secretion of infectious particles. In a first study, we highlighted the functional connection between replication complexes and assembly sites. In a second study, we showed that p7 dose-dependently slows down the ER-to-Golgi traffic, leading to intracellular retention of E2 viral glycoprotein. In addition, we showed that cleavage of an E2p7 precursor protein controls E2 intracellular expression and secretion levels of subviral particles and infectious virions. Finally, we also highlighted that p7 N-terminal extremity governs the specific infectivity of the infectious particles by coordinating the encountering of the nucleocapsid components with the glycoproteins and the envelopment of the nucleocapsids. In a third study, we discovered specific functions and factors from serum, producer cells, and HCV sequences that modulate lipidation of viral particles during their assembly and secretion. Altogether, these different works contributed at better understanding the steps of HCV assembly and the mechanisms modulating i) the transfer of viral RNAs from replication complexes to assembly sites, ii) the encountering of the nucleocapsids and glycoproteins followed by virion envelopment, and finally, iii) the acquisition of lipids by viral particles; Le virus de l'hépatite C (VHC) est détecté dans les sérums de patients infectés sous forme de particules infectieuses lipidées de très faibles densités. Le VHC est un virus enveloppé dont l'assemblage de particules virales se produit à la membrane du réticulum endoplasmique consécutivement au clivage séquentiel de sa polyprotéine et à sa maturation en protéines structurales et non structurales. Dans ce travail, nous avons cherché à mieux comprendre les mécanismes d'assemblage, d'enveloppement et de sécrétion des particules infectieuses. Dans une première étude, nous avons montré la connexion fonctionnelle entre les complexes de réplication et les sites d'assemblage. Dans une seconde étude, nous avons montré que p7 ralentissait de manière dose-dépendante le trafic ER-Golgi, conduisant à une rétention intracellulaire de la glycoprotéine virale E2. En outre, nous avons montré que le clivage du précurseur protéique E2p7 contrôle l'expression intracellulaire E2 et les niveaux de sécrétion des particules subvirales et des virions infectieux. Enfin, nous avons également mis en évidence que l'extrémité N-terminale de p7 gouverne l'infectivité spécifique des particules en coordonnant la rencontre des composants de la nucléocapside avec les glycoprotéines, mais aussi l'enveloppement de la nucléocapside. Dans une troisième étude, nous avons découvert des fonctions et des facteurs spécifiques du sérum, des cellules productrices et des séquences du VHC qui modulent la lipidation des particules virales au cours de leur assemblage et de leur sécrétion. Au total, ces différents travaux ont contribué à mieux comprendre les étapes de l'assemblage du VHC et les mécanismes modulant i) le transfert des ARN viraux des complexes de réplication vers les sites d’assemblage, ii) la rencontre des nucléocapsides et des glycoprotéines, et enfin, iii) l'acquisition de lipides par des particules virales

Published
2018

32. The amino-terminus of the hepatitis C virus (HCV) p7 viroporin and its cleavage from glycoprotein E2-p7 precursor determine specific infectivity and secretion levels of HCV particle types

Author

Denolly, Solène, Mialon, Chloé, Bourlet, Thomas, Amirache, Fouzia, Penin, François, Lindenbach, Brett, Boson, Bertrand, Cosset, François-Loïc, Virus enveloppés, vecteurs et immunothérapie – Enveloped viruses, Vectors and Immuno-therapy (EVIR), Centre International de Recherche en Infectiologie - UMR (CIRI), Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Groupe Immunité des Muqueuses et Agents Pathogènes (GIMAP), Université Jean Monnet [Saint-Étienne] (UJM), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Department of Microbial Pathogenesis, Yale University School of Medicine, Centre International de Recherche en Infectiologie (CIRI), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Jean Monnet - Saint-Étienne (UJM), and Yale School of Medicine [New Haven, Connecticut] (YSM)

Subjects
RNA viruses, Physiology, viruses, Hepacivirus, Viral Nonstructural Proteins, Pathology and Laboratory Medicine, Biochemistry, Virions, Viral Envelope Proteins, Models, Immune Physiology, Medicine and Health Sciences, lcsh:QH301-705.5, Immune System Proteins, Virulence, Hepatitis C virus, Medical microbiology, Hepatitis C, Protein Transport, Intracellular Pathogens, Cell Processes, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Viruses, Host-Pathogen Interactions, [SDV.IMM]Life Sciences [q-bio]/Immunology, Pathogens, Research Article, lcsh:Immunologic diseases. Allergy, Immunology, Viral Structure, Microbiology, Models, Biological, Antibodies, Cell Line, Viral Proteins, Virology, Viral Core, Humans, Amino Acid Sequence, Protein Processing, Secretion, Flaviviruses, Virus Assembly, Post-Translational, Organisms, Viral pathogens, Biology and Life Sciences, Proteins, Protein Secretion, Cell Biology, Biological, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Hepatitis viruses, Microbial pathogens, HEK293 Cells, lcsh:Biology (General), Mutation, lcsh:RC581-607, Physiological Processes, Protein Processing, Post-Translational
Abstract

Viroporins are small transmembrane proteins with ion channel activities modulating properties of intracellular membranes that have diverse proviral functions. Hepatitis C virus (HCV) encodes a viroporin, p7, acting during assembly, envelopment and secretion of viral particles (VP). HCV p7 is released from the viral polyprotein through cleavage at E2-p7 and p7-NS2 junctions by signal peptidase, but also exists as an E2p7 precursor, of poorly defined properties. Here, we found that ectopic p7 expression in HCVcc-infected cells reduced secretion of particle-associated E2 glycoproteins. Using biochemical assays, we show that p7 dose-dependently slows down the ER-to-Golgi traffic, leading to intracellular retention of E2, which suggested that timely E2p7 cleavage and p7 liberation are critical events to control E2 levels. By studying HCV mutants with accelerated E2p7 processing, we demonstrate that E2p7 cleavage controls E2 intracellular expression and secretion levels of nucleocapsid-free subviral particles and infectious virions. In addition, our imaging data reveal that, following p7 liberation, the amino-terminus of p7 is exposed towards the cytosol and coordinates the encounter between NS5A and NS2-based assembly sites loaded with E1E2 glycoproteins, which subsequently leads to nucleocapsid envelopment. We identify punctual mutants at p7 membrane interface that, by abrogating NS2/NS5A interaction, are defective for transmission of infectivity owing to decreased secretion of core and RNA and to increased secretion of non/partially-enveloped particles. Altogether, our results indicate that the retarded E2p7 precursor cleavage is essential to regulate the intracellular and secreted levels of E2 through p7-mediated modulation of the cell secretory pathway and to unmask critical novel assembly functions located at p7 amino-terminus., Author summary Viroporins are small transmembrane viral proteins with ion channel activities modulating properties of intracellular membranes, which impacts several fundamental biological processes such as trafficking, ion fluxes as well as connections and exchanges between organelles. Hepatitis C virus (HCV) encodes a viroporin, p7, acting during assembly, envelopment and secretion of viral particles. HCV p7 is produced by cleavage from the HCV polyprotein but also exists as an E2p7 precursor, of poorly defined properties. In this study, we have explored how the retarded cleavage between E2 glycoprotein and p7 viroporin could regulate their functions associated to virion assembly and/or perturbation of cellular membrane processes. Specifically, we demonstrate that p7 is able to regulate the cell secretory pathway, which induces the intracellular retention of HCV glycoproteins and favors assembly of HCV particles. Our study also identifies a novel assembly function located at p7 amino-terminus that is unmasked through E2p7-regulated processing and that controls the infectivity of different types of released viral particles. Altogether, our results underscore a critical post-translational control of assembly and secretion of HCV particles that governs their specific infectivity.

Published
2017
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34. Daclatasvir Prevents Hepatitis C Virus by Blocking Transfer of Viral Genome to Assembly Sites

Author

Boson, Bertrand, Denolly, Solène, Turlure, Fanny, Chamot, Christophe, Dreux, Marlène, Cosset, François-Loïc, Centre International de Recherche en Infectiologie (CIRI), Centre National de la Recherche Scientifique (CNRS) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Université Claude Bernard Lyon 1 (UCBL) - École normale supérieure - Lyon (ENS Lyon), BioSciences Gerland - Lyon Sud, and École normale supérieure - Lyon (ENS Lyon) - Université Claude Bernard Lyon 1 (UCBL) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Centre National de la Recherche Scientifique (CNRS)

Subjects
direct-acting antiviral agent, viruses, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, virus diseases, chronic hepatitis C, digestive system diseases, [SDV.MHEP.HEG] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, DAA
Abstract

International audience; Daclatasvir is a direct-acting antiviral agent and potent inhibitor of NS5A, which is involved in replication of the hepatitis C virus (HCV) genome, presumably via membranous web shaping, and assembly of new virions, likely via transfer of the HCV RNA genome to viral particle assembly sites. Daclatasvir inhibits the formation of new membranous web structures and, ultimately, of replication complex vesicles, but also inhibits an early assembly step. We investigated the relationship between daclatasvir-induced clustering of HCV proteins, intracellular localization of viral RNAs and inhibition of viral particle assembly.; HCVcc particles were produced from Huh7.5 hepatocarcinoma cells in presence of daclatasvir for short time periods. Infectivity as well as production of physical particles were quantified and producer cells were subjected to subcellular fractionation. Intracellular colocalization between core, E2, NS5A, NS4B proteins, and viral RNAs was quantitatively analyzed by confocal microscopy and by structured illumination microscopy.; Short exposure of HCV-infected cells to daclatasvir reduced viral assembly and induced clustering of structural proteins with non-structural HCV proteins, including core, E2, NS4B and NS5A. These clustered structures appeared to be inactive assembly platforms, likely owing to loss of functional connection with replication complexes. Daclatasvir greatly reduced delivery of viral genomes to these core clusters without altering HCV RNA colocalization with NS5A. In contrast, daclatasvir neither induced clustered structures nor inhibited HCV assembly in cells infected with a daclatasvir-resistant mutant (NS5A-Y93H), indicating that daclatasvir targets a mutual, specific function of NS5A inhibiting both processes.; In addition to inhibiting replication complex biogenesis, daclatasvir prevents viral assembly by blocking transfer of the viral genome to assembly sites. This leads to clustering of HCV proteins, because viral particles and replication complex vesicles cannot form and/or egress. This dual mode of action of daclatasvir could explain its efficacy in blocking HCV replication in cultured cells and in treatment of patients with HCV infection.

Published
2016
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36. A Large‐Scale Serological Survey in Pets From October 2020 Through June 2021 in France Shows Significantly Higher Exposure to SARS‐CoV‐2 in Cats Compared to Dogs.

Author

Fritz, Matthieu, Elguero, Eric, Becquart, Pierre, De Riols de Fonclare, Daphné, Garcia, Déborah, Beurlet, Stephanie, Denolly, Solène, Boson, Bertrand, Rosolen, Serge G., Cosset, François‐Loïc, Briend‐Marchal, Alexandra, Legros, Vincent, and Leroy, Eric M.

Subjects
*SARS-CoV-2, *PETS, *DOMESTIC animals, *STATISTICAL reliability, *PERIODIC health examinations, *DOGS, *CATS
Abstract

ABSTRACT Introduction Methods Results Conclusions Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) has the potential to infect various animals, including domestic pets like dogs and cats. Many studies have documented infection in companion animals by molecular and serological methods. However, only a few have compared seroprevalence in cats and dogs from the general population, and these studies were limited by small sample sizes and collections over short periods. Our aim was to obtain a more accurate evaluation of seroprevalence in companion animals in France and to determine whether cats and dogs differ in their exposure to SARS‐CoV‐2.We conducted an extensive serological survey of SARS‐CoV‐2, collecting blood samples from 2036 cats and 3577 dogs during routine veterinary medical examinations across different regions of metropolitan France from October 2020 to June 2021. This period encompassed the peaks and onset of two waves, as well as the emergence of the first variants. A microsphere immunoassay targeting the receptor‐binding domain and trimeric spike protein was used to detect anti‐SARS‐CoV‐2 antibodies. A subset of 308 seropositive samples was tested for the presence of neutralising antibodies.We determined an overall seroprevalence of anti‐SARS‐CoV‐2 antibodies of 7.1% (95% confidence interval [CI]: 6.4%–7.8%) among the sampled pets. Cats exhibited a significantly higher seroprevalence (9.3%; 95% CI: 8.1%–10.1%) compared to dogs (5.9%; 95% CI: 5.2%–6.8%). Among the subset of seropositive samples, 81 (26.3%; 95% CI: 21.5%–31.6%) displayed neutralizing antibodies. Furthermore, seroprevalence in both species was lower in older animals and was not associated with sex. Finally, unlike cats, seroprevalence in dogs was found to be correlated with the date of sampling.The large sample size enhances the reliability and statistical robustness of our estimates regarding pet exposure to SARS‐CoV‐2. This study on SARS‐CoV‐2 reaffirms the crucial importance of adopting a One Health approach incorporating domestic animals when managing an epidemic caused by a zoonotic virus. [ABSTRACT FROM AUTHOR]

Published
2024
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37. Pan-serotype dengue virus inhibitor JNJ-A07 targets NS4A-2K-NS4B interaction with NS2B/NS3 and blocks replication organelle formation.

Author

Kiemel D, Kroell AH, Denolly S, Haselmann U, Bonfanti JF, Andres JI, Ghosh B, Geluykens P, Kaptein SJF, Wilken L, Scaturro P, Neyts J, Van Loock M, Goethals O, and Bartenschlager R

Subjects
Humans, Serogroup, RNA Helicases metabolism, RNA Helicases antagonists & inhibitors, RNA Helicases genetics, Serine Endopeptidases metabolism, Serine Endopeptidases genetics, Protein Binding, Animals, Organelles metabolism, Organelles drug effects, Viral Proteases, Aminophenols, Membrane Proteins, Indoles, DEAD-box RNA Helicases, Nucleoside-Triphosphatase, Butyrates, Dengue Virus drug effects, Dengue Virus genetics, Dengue Virus physiology, Viral Nonstructural Proteins metabolism, Viral Nonstructural Proteins genetics, Viral Nonstructural Proteins antagonists & inhibitors, Virus Replication drug effects, Antiviral Agents pharmacology, Dengue virology, Dengue drug therapy
Abstract

Dengue fever represents a significant medical and socio-economic burden in (sub)tropical regions, yet antivirals for treatment or prophylaxis are lacking. JNJ-A07 was described as highly active against the different genotypes within each serotype of the disease-causing dengue virus (DENV). Based on clustering of resistance mutations it has been assumed to target DENV non-structural protein 4B (NS4B). Using a photoaffinity labeling compound with high structural similarity to JNJ-A07, here we demonstrate binding to NS4B and its precursor NS4A-2K-NS4B. Consistently, we report recruitment of the compound to intracellular sites enriched for these proteins. We further specify the mechanism-of-action of JNJ-A07, which has virtually no effect on viral polyprotein cleavage, but targets the interaction between the NS2B/NS3 protease/helicase complex and the NS4A-2K-NS4B cleavage intermediate. This interaction is functionally linked to de novo formation of vesicle packets (VPs), the sites of DENV RNA replication. JNJ-A07 blocks VPs biogenesis with little effect on established ones. A similar mechanism-of-action was found for another NS4B inhibitor, NITD-688. In summary, we unravel the antiviral mechanism of these NS4B-targeting molecules and show how DENV employs a short-lived cleavage intermediate to carry out an early step of the viral life cycle., (© 2024. The Author(s).)

Published
2024
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38. [The hepatitis delta virus: an easily turncoat pathogen?]

Author

Vignon A, Denolly S, Perez-Vargas J, and Cosset FL

Subjects
Animals, Coinfection, Hepatitis B complications, Hepatitis B virology, Hepatitis D complications, Hepatitis Delta Virus pathogenicity, Humans, Hepatitis B virus physiology, Hepatitis D virology, Hepatitis Delta Virus physiology, Virus Release physiology, Virus Replication physiology
Published
2020
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39. [Extracellular maturation of hepatitis C virus: a plasma cloak of invisibility].

Author

Chanut M, Granier C, Cosset FL, and Denolly S

Subjects
Antibodies, Neutralizing metabolism, Hepacivirus genetics, Hepacivirus immunology, Hepacivirus ultrastructure, Hepatitis C blood, Hepatitis C immunology, Hepatitis C virology, Hepatitis C Antibodies metabolism, Hepatitis C Antigens metabolism, Host-Pathogen Interactions, Humans, Surface Properties, Viral Envelope Proteins genetics, Viral Envelope Proteins physiology, Viremia blood, Viremia immunology, Viremia virology, Virion physiology, Virion ultrastructure, Antibodies, Neutralizing immunology, Hepacivirus physiology, Hepatitis C Antibodies immunology, Hepatitis C Antigens immunology, Lipoproteins blood, Viral Envelope Proteins immunology
Published
2019
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40. Membrane Fusion Assays for Studying Entry Hepatitis C Virus into Cells.

Author

Denolly S, Cosset FL, and Freitas N

Subjects
Antiviral Agents pharmacology, Cell Culture Techniques methods, Cell Line, Glycoproteins metabolism, HEK293 Cells, Hepacivirus drug effects, Hepatitis C drug therapy, Hepatitis C metabolism, Humans, Liposomes chemistry, Liposomes metabolism, Transfection methods, Virion drug effects, Virion physiology, Hepacivirus physiology, Hepatitis C pathology, Host-Pathogen Interactions drug effects, Membrane Fusion drug effects, Virus Internalization drug effects
Abstract

The membrane fusion properties of HCV envelope glycoproteins can be evaluated using several assays. Fusion assays generally require contacts between glycoproteins expressed on a donor membrane, such as those from a cell or a viral particle, and an acceptor membrane that may or may not express cognate viral receptor, such as those from an indicator cell or a liposome. In this chapter, we describe three well-established methods in the field that use either cell surface expression of glycoproteins, HCV pseudoparticles (HCVpp), or cell culture-grown HCV (HCVcc) particles for donor membrane and cells or liposomes as acceptor membrane in which specific components can be included to monitor and quantify fusion. We provide details of cell-cell fusion assay, virus-liposome fusion assay, and finally virus-plasma membrane fusion assay. We also describe inhibitors that can block HCV envelope membrane fusion.

Published
2019
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