ArticlemBio2017
Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2.
Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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
26 citing papers in PubMed, 33 citations in OpenAlex.
- Targets of protective immunity and opportunities in hepatitis C virus vaccine development.Nature reviews. Immunology · 2026Review
- Human tetraspanin CD81 facilitates invasion ofVirulence · 2024Article
- Current Hepatitis C Vaccine Candidates Based on the Induction of Neutralizing Antibodies.Viruses · 2023Review
- Article
- Viral Glycoproteins Induce NLRP3 Inflammasome Activation and Pyroptosis in Macrophages.Viruses · 2021Article
- Structural and Biophysical Characterization of the HCV E1E2 Heterodimer for Vaccine Development.Viruses · 2021Review
- From Structural Studies to HCV Vaccine Design.Viruses · 2021Review
- Design and Synthesis of HCV-E2 Glycoprotein Epitope Mimics in Molecular Construction of Potential Synthetic Vaccines.Viruses · 2021Article
- On Origin and Evolution of the Antibody Molecule.Biology · 2021Review
- Design of a native-like secreted form of the hepatitis C virus E1E2 heterodimer.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Optimized cell systems for the investigation of hepatitis C virus E1E2 glycoproteins.The Journal of general virology · 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
- Article
- Article
- Flexibility and intrinsic disorder are conserved features of hepatitis C virus E2 glycoprotein.PLoS computational biology · 2020Article
- Improving the aqueous solubility of HCV-E2 glycoprotein epitope mimics by cyclization using POLAR hinges.Journal of peptide science : an official publication of the European Peptide Society · 2020Article
- Novel adeno‑associated virus‑based genetic vaccines encoding hepatitis C virus E2 glycoprotein elicit humoral immune responses in mice.Molecular medicine reports · 2019Article
- Article
- Synergistic anti-HCV broadly neutralizing human monoclonal antibodies with independent mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 4 countries.
Funding
Abstract
The hepatitis C virus (HCV) glycoprotein E2 is the major target of neutralizing antibodies and is therefore highly relevant for vaccine design. Its structure features a central immunoglobulin (Ig)-like β-sandwich that contributes to the binding site for the cellular receptor CD81. We show that a synthetic peptide corresponding to a β-strand of this Ig-like domain forms an α-helix in complex with the anti-E2 antibody DAO5, demonstrating an inside-out flip of hydrophobic residues and a secondary structure change in the composite CD81 binding site. A detailed interaction analysis of DAO5 and cross-competing neutralizing antibodies with soluble E2 revealed that the Ig-like domain is trapped by different antibodies in at least two distinct conformations. DAO5 specifically captures retrovirus particles bearing HCV glycoproteins (HCVpp) and infectious cell culture-derived HCV particles (HCVcc). Infection of cells by DAO5-captured HCVpp can be blocked by a cross-competing neutralizing antibody, indicating that a single virus particle simultaneously displays E2 molecules in more than one conformation on its surface. Such conformational plasticity of the HCV E2 receptor binding site has important implications for immunogen design.
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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.