Year: 2018
Type: article
Abstract: HCV is a major public health problem worldwide. The virion harbors two envelope proteins, E1 and E2, which are involved at different steps of the viral life cycle. Whereas E2 has been extensively characterized, the function of E1 remains poorly defined. We characterized here the function of the putative fusion peptide and the region containing α helices of the E1 ectodomain, which had been previously suggested to be important for virus entry. We could confirm the importance of these regions for the virus infectivity. Interestingly, we found several residues modulating the virus's dependence on several HCV receptors, thus highlighting the role of E1 in the interaction of the virus with cellular receptors. Whereas mutations in the putative fusion peptide affected HCV infectivity and morphogenesis, several mutations in the α2-helix region led to a loss of infectivity with no effect on assembly, indicating a role of this region in virus entry.
Source: Journal of Virology
DOI: 10.1128/jvi.00939-18
Institutions: Centre National de la Recherche Scientifique, Inserm, Institut Pasteur de Lille, Centre Hospitalier Universitaire de Lille, Center for Infection and Immunity of Lille, National Research Centre, Lebanese University, Université de Lille, Unité de Glycobiologie Structurale et Fonctionnelle, Centre Hospitalier Universitaire Amiens-Picardie, Agents infectieux, résistance et chimiothérapie, Université de Picardie Jules Verne, Ghent University, Hôpitaux Universitaires de Strasbourg, Institute for Translational Medicine and Liver Disease, Université de Strasbourg
Language: English
Topic: Hepatitis C virus research
Subfield: Hepatology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W2885641715