ArticleJournal of virology2015
A view of the E2-CD81 interface at the binding site of a neutralizing antibody against hepatitis C virus.
Article in Journal of virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Structural and genetic signatures of two classes of HCV E2 neutralizing face antibodies from non-human primates immunized with a recombinant E1E2.NPJ vaccines · 2026Article
- Hepatitis C virus modifiedJournal of virology · 2025Article
- Human tetraspanin CD81 facilitates invasion ofVirulence · 2024Article
- Evolutionary modeling reveals enhanced mutational flexibility of HCV subtype 1b compared with 1a.iScience · 2022Article
- A conserved epitope III on hepatitis C virus E2 protein has alternate conformations facilitating cell binding or virus neutralization.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- In vitro adaptation and characterization of attenuated hypervariable region 1 swap chimeras of hepatitis C virus.PLoS pathogens · 2021Article
- Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus.PloS one · 2021Article
- Clearance of hepatitis C virus is associated with early and potent but narrowly-directed, Envelope-specific antibodies.Scientific reports · 2019Article
- Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.Frontiers in immunology · 2018Review
- Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.Frontiers in immunology · 2018Review
- A mutation in the human tetraspanin CD81 gene is expressed as a truncated protein but does not enable CD19 maturation and cell surface expression.Journal of clinical immunology · 2015Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledHepatitis C virus (HCV) glycoprotein E2 is considered a major target for generating neutralizing antibodies against HCV, primarily due to its role of engaging host entry factors, such as CD81, a key cell surface protein associated with HCV entry. Based on a series of biochemical analyses in combination with molecular docking, we present a description of a potential binding interface formed between the E2 protein and CD81. The virus side of this interface includes a hydrophobic helix motif comprised of residues W(437)LAGLF(442), which encompasses the binding site of a neutralizing monoclonal antibody, mAb41. The helical conformation of this motif provides a structural framework for the positioning of residues F442 and Y443, serving as contact points for the interaction with CD81. The cell side of this interface likewise involves a surface-exposed hydrophobic helix, namely, the D-helix of CD81, which coincides with the binding site of 1D6, a monoclonal anti-CD81 antibody known to block HCV entry. Our illustration of this virus-host interface suggests an important role played by the W(437)LAGLF(442) helix of the E2 protein in the hydrophobic interaction with the D-helix of CD81, thereby facilitating our understanding of the mechanism for antibody-mediated neutralization of HCV. IMPORTANCE: Characterization of the interface established between a virus and host cells can provide important information that may be used for the control of virus infections. The interface that enables hepatitis C virus (HCV) to infect human liver cells has not been well understood because of the number of cell surface proteins, factors, and conditions found to be associated with the infection process. Based on a series of biochemical analyses in combination with molecular docking, we present such an interface, consisting of two hydrophobic helical structures, from the HCV E2 surface glycoprotein and the CD81 protein, a major host cell receptor recognized by all HCV strains. Our study reveals the critical role played by hydrophobic interactions in the formation of this virus-host interface, thereby contributing to our understanding of the mechanism for antibody-mediated neutralization of HCV.
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