ArticleJournal of virology2012
Amino acid residue-specific neutralization and nonneutralization of hepatitis C virus by monoclonal antibodies to the E2 protein.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 30 citations in OpenAlex.
- 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
- Antibody responses to a highly conserved peptide in HCV E2 protein correlate with chronicity or spontaneous clearance of HCV infection.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cell-Free Display Techniques for Protein Evolution.Advances in biochemical engineering/biotechnology · 2023Article
- Directing evolution of novel ligands by mRNA display.Chemical Society reviews · 2021Review
- 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
- From Structural Studies to HCV Vaccine Design.Viruses · 2021Review
- Review
- Antibody Responses in Hepatitis C Infection.Cold Spring Harbor perspectives in medicine · 2021Review
- HCV Glycoprotein Structure and Implications for B-Cell Vaccine Development.International journal of molecular sciences · 2020Review
- An alternate conformation of HCV E2 neutralizing face as an additional vaccine target.Science advances · 2020Article
- Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.Frontiers in immunology · 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
- Innate and Adaptive Immune Responses in Chronic HCV Infection.Current drug targets · 2017Review
- Reverse Engineering of Vaccine Antigens Using High Throughput Sequencing-enhanced mRNA Display.EBioMedicine · 2015Article
- A view of the E2-CD81 interface at the binding site of a neutralizing antibody against hepatitis C virus.Journal of virology · 2015Article
- Immune control and failure in HCV infection--tipping the balance.Journal of leukocyte biology · 2014Review
- Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies to epitopes in the E2 protein of hepatitis C virus (HCV) reduce the viral infectivity in vivo and in vitro. However, the virus can persist in patients in the presence of neutralizing antibodies. In this study, we generated a panel of monoclonal antibodies that bound specifically to the region between residues 427 and 446 of the E2 protein of HCV genotype 1a, and we examined their capacity to neutralize HCV in a cell culture system. Of the four monoclonal antibodies described here, two were able to neutralize the virus in a genotype 1a-specific manner. The other two failed to neutralize the virus. Moreover, one of the nonneutralizing antibodies could interfere with the neutralizing activity of a chimpanzee polyclonal antibody at E2 residues 412 to 426, as it did with an HCV-specific immune globulin preparation, which was derived from the pooled plasma of chronic hepatitis C patients. Mapping the epitope-paratope contact interfaces revealed that these functionally distinct antibodies shared binding specificity for key amino acid residues, including W(437), L(438), L(441), and F(442), within the same epitope of the E2 protein. These data suggest that the effectiveness of antibody-mediated neutralization of HCV could be deduced from the interplay between an antibody and a specific set of amino acid residues. Further understanding of the molecular mechanisms of antibody-mediated neutralization and nonneutralization should provide insights for designing a vaccine to control HCV infection in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.