ArticleProceedings of the National Academy of Sciences of the United States of America2014
Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Antibodies to an interfering epitope in hepatitis C virus E2 can mask vaccine-induced neutralizing activity.Hepatology (Baltimore, Md.) · 2015Trial
- Targets of protective immunity and opportunities in hepatitis C virus vaccine development.Nature reviews. Immunology · 2026Review
- 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
- Structural and Biophysical Characterization of the HCV E1E2 Heterodimer for Vaccine Development.Viruses · 2021Review
- From Structural Studies to HCV Vaccine Design.Viruses · 2021Review
- Review
- Characterization of linear epitope specificity of antibodies potentially contributing to spontaneous clearance of hepatitis C virus.PloS one · 2021Article
- HCV Glycoprotein Structure and Implications for B-Cell Vaccine Development.International journal of molecular sciences · 2020Review
- Hepatitis C virus vaccine design: focus on the humoral immune response.Journal of biomedical science · 2020Review
- Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing Epitopes.Journal of virology · 2020Article
- Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoprotein.PLoS computational biology · 2020Article
- Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018Review
- The Neutralizing Face of Hepatitis C Virus E2 Envelope Glycoprotein.Frontiers in immunology · 2018Review
- Predicting the Effectiveness of Hepatitis C Virus Neutralizing Antibodies by Bioinformatic Analysis of Conserved Epitope Residues Using Public Sequence Data.Frontiers in immunology · 2018Article
- Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.Frontiers in immunology · 2018Review
- Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.Frontiers in immunology · 2018Review
- Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.Frontiers in immunology · 2018Review
- Antibody-Mediated Catalysis in Infection and Immunity.Infection and immunity · 2017Review
- Article
- Designing a B Cell-Based Vaccine against a Highly Variable Hepatitis C Virus.Frontiers in microbiology · 2017Review
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Authors and funding
10 authors.
Funding
Abstract
The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.
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