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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 05 July 2016, Vol.113(27), pp.7298-300
    Description: Author contributions: C.C.C., J.L., and T.F.B. wrote the paper.
    Keywords: Cadherins ; Hepacivirus
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    In: The New England Journal of Medicine, 2014, Vol.370(17), pp.1576-1578
    Description: The development of direct-acting antiviral agents has revolutionized the treatment of hepatitis C by offering genuine prospects for a comprehensive cure of a chronic viral infection. This success can be traced to important scientific, clinical, and regulatory developments. Chronic hepatitis C is a major cause of liver cirrhosis and hepatocellular carcinoma worldwide. Some 130 million to 170 million people, or about 3% of the world's population, are chronically infected with the hepatitis C virus (HCV). In the United States, chronic hepatitis C, the most common cause of liver-related death and reason for liver transplantation, recently eclipsed human immunodeficiency virus (HIV) infection as a cause of death. The development of direct-acting antiviral agents (DAAs) has revolutionized HCV treatment by offering genuine prospects for the first comprehensive cure of a chronic viral infection in humans. This success can be traced . . .
    Keywords: United States–Us ; Chronic Infection ; Antiviral Drugs ; Hepatitis C ; Antiviral Agents ; Drug Therapy ; Hepatitis ; Food & Drug Administration–FDA;
    ISSN: 0028-4793
    E-ISSN: 1533-4406
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  • 3
    Language: English
    In: The Lancet, 18 February 2017, Vol.389(10070), pp.674-675
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/S0140-6736(17)30043-0 Byline: Mirjam B Zeisel (a)(b), Thomas F Baumert (a)(b)(c) Author Affiliation: (a) Institut National de la Sante et de la Recherche Medicale, U1110, Institut de Recherche sur les Maladies Virales et Hepatiques, Strasbourg F-67000, France (b) Universite de Strasbourg, Strasbourg, France (c) Institut Hospitalo-Universitaire, Pole hepato-digestif, Nouvel Hopital Civil, Strasbourg, France
    Keywords: Medicine
    ISSN: 0140-6736
    E-ISSN: 1474-547X
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  • 4
    Language: English
    In: Gastroenterology, January 2017, Vol.152(1), pp.21-23
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1053/j.gastro.2016.11.029 Byline: Che C. Colpitts Author Affiliation: Inserm, U1110, Institut de Recherche sur les Maladies Virales et Hepatiques and Universite de Strasbourg, Strasbourg, France Article Note: (footnote) Conflicts of interest The authors disclose no conflicts., TFB acknowledges support from the National Institutes of Health (NIAID U19 AI123862-01), the European Union (ERC-2014-AdG-671231-HEPCIR, FP7 HepaMAb, EU H2020 HepCAR), the French Cancer Agency (ARC IHU201301187), and ANR (LABEX ANR-10-LAB-28). CCC acknowledges fellowships from the Canadian Institutes of Health Research (201411MFE-338606-245517) and the Canadian Network on Hepatitis C.
    Keywords: Medicine
    ISSN: 0016-5085
    E-ISSN: 1528-0012
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  • 5
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 06 August 2013, Vol.110(32), pp.13109-13
    Description: Recent evidence indicates there is a role for small membrane vesicles, including exosomes, as vehicles for intercellular communication. Exosomes secreted by most cell types can mediate transfer of proteins, mRNAs, and microRNAs, but their role in the transmission of infectious agents is less established. Recent studies have shown that hepatocyte-derived exosomes containing hepatitis C virus (HCV) RNA can activate innate immune cells, but the role of exosomes in the transmission of HCV between hepatocytes remains unknown. In this study, we investigated whether exosomes transfer HCV in the presence of neutralizing antibodies. Purified exosomes isolated from HCV-infected human hepatoma Huh7.5.1 cells were shown to contain full-length viral RNA, viral protein, and particles, as determined by RT-PCR, mass spectrometry, and transmission electron microscopy. Exosomes from HCV-infected cells were capable of transmitting infection to naive human hepatoma Huh7.5.1 cells and establishing a productive infection. Even with subgenomic replicons, lacking structural viral proteins, exosome-mediated transmission of HCV RNA was observed. Treatment with patient-derived IgGs showed a variable degree of neutralization of exosome-mediated infection compared with free virus. In conclusion, this study showed that hepatic exosomes can transmit productive HCV infection in vitro and are partially resistant to antibody neutralization. This discovery sheds light on neutralizing antibodies resistant to HCV transmission by exosomes as a potential immune evasion mechanism.
    Keywords: Exosomes -- Virology ; Hepacivirus -- Genetics ; RNA, Viral -- Genetics ; Virion -- Genetics
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 6
    Language: English
    In: Proceedings of the National Academy of Sciences, 11/08/2016, Vol.113(45), pp.E6946-E6954
    Description: The E2 envelope glycoprotein is the primary target of human neutralizing antibody response against hepatitis C virus (HCV), and is thus a major focus of vaccine and immunotherapeutics efforts. There is emerging evidence that E2 is a highly complex, dynamic protein with residues across the protein that are modulating antibody recognition, local and global E2 stability, and viral escape. To comprehensively map these determinants, we performed global E2 alanine scanning with a panel of 16 human monoclonal antibodies (hmAbs), resulting in an unprecedented dataset of the effects of individual alanine substitutions across the E2 protein (355 positions) on antibody recognition. Analysis of shared energetic effects across the antibody panel identified networks of E2 residues involved in antibody recognition and local and global E2 stability, as well as predicted contacts between residues across the entire E2 protein. Further analysis of antibody binding hotspot residues defined groups of residues essential for E2 conformation and recognition for all 14 conformationally dependent E2 antibodies and subsets thereof, as well as residues that enhance antibody recognition when mutated to alanine, providing a potential route to engineer E2 vaccine immunogens. By incorporating E2 sequence variability, we found a number of E2 polymorphic sites that are responsible for loss of neutralizing antibody binding. These data and analyses provide fundamental insights into antibody recognition of E2, highlighting the dynamic and complex nature of this viral envelope glycoprotein, and can serve as a reference for development and rational design of E2-targeting vaccines and immunotherapeutics.
    Keywords: Data Processing ; Envelopes ; Alanine ; Monoclonal Antibodies ; Hot Spots ; E2 Protein ; Antibody Response ; Mapping ; Glycoproteins ; Vaccines ; Mutagenesis ; Hepatitis C Virus ; Vaccines ; Immunology;
    ISSN: 0027-8424
    E-ISSN: 1091-6490
    Source: CrossRef
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  • 7
    Language: English
    In: Gastroenterology, July 2012, Vol.143(1), pp.223-233.e9
    Description: The development of vaccines and other strategies to prevent hepatitis C virus (HCV) infection is limited by rapid viral evasion. HCV entry is the first step of infection; this process involves several viral and host factors and is targeted by host-neutralizing responses. Although the roles of host factors in HCV entry have been well characterized, their involvement in evasion of immune responses is poorly understood. We used acute infection of liver graft as a model to investigate the molecular mechanisms of viral evasion. We studied factors that contribute to evasion of host immune responses using patient-derived antibodies, HCV pseudoparticles, and cell culture–derived HCV that express viral envelopes from patients who have undergone liver transplantation. These viruses were used to infect hepatoma cell lines that express different levels of HCV entry factors. By using reverse genetic analyses, we identified altered use of host-cell entry factors as a mechanism by which HCV evades host immune responses. Mutations that alter use of the CD81 receptor also allowed the virus to escape neutralizing antibodies. Kinetic studies showed that these mutations affect virus–antibody interactions during postbinding steps of the HCV entry process. Functional studies with a large panel of patient-derived antibodies showed that this mechanism mediates viral escape, leading to persistent infection in general. We identified a mechanism by which HCV evades host immune responses, in which use of cell entry factors evolves with escape from neutralizing antibodies. These findings advance our understanding of the pathogenesis of HCV infection and might be used to develop antiviral strategies and vaccines.
    Keywords: Virology ; Liver Disease ; Tissue Culture Model ; Immunity ; Medicine
    ISSN: 0016-5085
    E-ISSN: 1528-0012
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  • 8
    Article
    Article
    BMJ Publishing Group Ltd and British Society of Gastroenterology
    Language: English
    In: Gut, 8 March 2019, Vol.68(3), p.547
    Description: Over the past two decades a growing body of evidence has demonstrated an important role of tight junction (TJ) proteins in the physiology and disease biology of GI and liver disease. On one side, TJ proteins exert their functional role as integral proteins of TJs in forming barriers in the gut and the liver. Furthermore, TJ proteins can also be expressed outside TJs where they play important functional roles in signalling, trafficking and regulation of gene expression. A hallmark of TJ proteins in disease biology is their functional role in epithelial-to-mesenchymal transition. A causative role of TJ proteins has been established in the pathogenesis of colorectal cancer and gastric cancer. Among the best characterised roles of TJ proteins in liver disease biology is their function as cell entry receptors for HCV—one of the most common causes of hepatocellular carcinoma. At the same time TJ proteins are emerging as targets for novel therapeutic approaches for GI and liver disease. Here we review our current knowledge of the role of TJ proteins in the pathogenesis of GI and liver disease biology and discuss their potential as therapeutic targets.
    Keywords: Hepatitis C ; Hepatocellular Carcinoma ; Colorectal Cancer ; Tight Junction
    ISSN: 0017-5749
    ISSN: 00175749
    E-ISSN: 1468-3288
    E-ISSN: 14683288
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  • 9
    Language: English
    In: The Journal of infectious diseases, 01 December 2013, Vol.208(11), pp.1888-97
    Description: The envelope glycoprotein E2 of hepatitis C virus (HCV) contains several hypervariable regions. Interestingly, 2 regions of intragenotypic hypervariability within E2 have been described as being specific to HCV subtype 3a. Based on their amino acid position in E2, they were named HVR495 and HVR575. Here, we further investigated these regions in order to better understand their role in HCV infection. Sequences of HCV envelope glycoproteins from Pakistani patients infected with subtype 3a were cloned and compared with other subtype 3a sequences. The entry functions and the sensitivity to antibody neutralization of selected HCV glycoprotein sequences were tested in the HCV pseudotyped particles (HCVpp) system. In addition, the cell-cultured HCV system (HCVcc) was also used to confirm some of the data obtained with the HCVpp system. We observed interesting new features within HVR495 and HVR575 for several subtype 3a isolates. Indeed, changes in glycosylation sites were observed with the appearance of a new glycosylation site within HVR495. Importantly, HCVpp and HCVcc that contained this new HVR495 glycosylation site were less sensitive to antibody neutralization. We identified a new glycosylation site within the HVR495 region of HCV subtype 3a that has a protective effect against antibody neutralization.
    Keywords: Hepacivirus ; Hepatitis C Virus ; Neutralizing Antibodies ; Sequence Variability ; Viral Glycoproteins ; Antibodies, Neutralizing -- Immunology ; Epitopes -- Immunology ; Hepacivirus -- Immunology ; Hepatitis C -- Virology ; Hepatitis C Antibodies -- Immunology ; Viral Envelope Proteins -- Chemistry
    ISSN: 00221899
    E-ISSN: 1537-6613
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  • 10
    In: The Journal of Virology, 2010, Vol. 84(17), p.8964
    Description: Dendritic cells (DCs) are of pivotal importance for the initiation of immune responses to control and eliminate viral infections. The molecular mechanisms of hepatitis C virus (HCV) antigen uptake and processing by blood DCs are poorly defined. Here we show that human blood DC subsets acquire HCV independent of the classical HCV entry factors. Following HCV uptake, human plasmacytoid and myeloid DC subsets deliver HCV antigen into distinct endocytotic compartments, which are dedicated to presentation to CD4(+) or CD8(+) T cells. Our findings support a model of HCV antigen processing and presentation in which DC subsets fulfill distinct functions.
    Keywords: Dendritic Cells -- Immunology ; Hepacivirus -- Immunology ; Hepatitis C -- Immunology ; Myeloid Cells -- Virology;
    ISSN: 0022-538X
    ISSN: 0022538X
    E-ISSN: 10985514
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