ArticleJournal of virology1997
Formation of native hepatitis C virus glycoprotein complexes.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 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
114 citing papers in PubMed, 314 citations in OpenAlex.
- Adapting in-cell ELISA to investigate the localization of hepatitis C virus envelope glycoproteins.Microbiology spectrum · 2026Article
- Alterations in N-glycosylation of HCV E2 Protein in Children Patients with IFN-RBV Therapy Failure.Pathogens (Basel, Switzerland) · 2024Article
- Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodies.Nature communications · 2023Article
- Current Hepatitis C Vaccine Candidates Based on the Induction of Neutralizing Antibodies.Viruses · 2023Review
- HCV E1 influences the fitness landscape of E2 and may enhance escape from E2-specific antibodies.Virus evolution · 2023Article
- Structure of the hepatitis C virus E1E2 glycoprotein complex.Science (New York, N.Y.) · 2022Article
- Incorporation of apolipoprotein E into HBV-HCV subviral envelope particles to improve the hepatitis vaccine strategy.Scientific reports · 2021Article
- The Molecular Basis for EViruses · 2021Article
- Interaction of Pestiviral E1 and E2 Sequences in Dimer Formation and Intracellular Retention.International journal of molecular sciences · 2021Article
- Antigenic and immunogenic evaluation of permutations of soluble hepatitis C virus envelope protein E2 and E1 antigens.PloS one · 2021Article
- Enhancing the antigenicity and immunogenicity of monomeric forms of hepatitis C virus E2 for use as a preventive vaccine.The Journal of biological chemistry · 2020Article
- Developments in the HCV Screening Technologies Based on the Detection of Antigens and Antibodies.Sensors (Basel, Switzerland) · 2019Review
- Functional expression and characterization of the envelope glycoprotein E1E2 heterodimer of hepatitis C virus.PLoS pathogens · 2019Article
- Role of Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly.Frontiers in immunology · 2018Review
- Hypervariable Region 1 in Envelope Protein 2 of Hepatitis C Virus: A Linchpin in Neutralizing Antibody Evasion and Viral Entry.Frontiers in immunology · 2018Review
- Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.Frontiers in immunology · 2018Review
- The amino-terminus of the hepatitis C virus (HCV) p7 viroporin and its cleavage from glycoprotein E2-p7 precursor determine specific infectivity and secretion levels of HCV particle types.PLoS pathogens · 2017Article
- Identification of Novel Functions for Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly.Journal of virology · 2017Article
- The core domain of hepatitis C virus glycoprotein E2 generates potent cross-neutralizing antibodies in guinea pigs.Hepatology (Baltimore, Md.) · 2017Article
- A Biologically-validated HCV E1E2 Heterodimer Structural Model.Scientific reports · 2017Article
54 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The hepatitis C virus (HCV) glycoproteins (E1 and E2) interact to form a heterodimeric complex, which has been proposed as a functional subunit of the HCV virion envelope. As examined in cell culture transient-expression assays, the formation of properly folded, noncovalently associated E1E2 complexes is a slow and inefficient process. Due to lack of appropriate immunological reagents, it has been difficult to distinguish between glycoprotein molecules that undergo productive folding and assembly from those which follow a nonproductive pathway leading to misfolding and aggregation. Here we report the isolation and characterization of a conformation-sensitive E2-reactive monoclonal antibody (H2). The H2 monoclonal antibody selectively recognizes slowly maturing E1E2 heterodimers which are noncovalently linked, protease resistant, and no longer associated with the endoplasmic reticulum chaperone calnexin. This complex probably represents the native prebudding form of the HCV glycoprotein heterodimer. Besides providing a novel reagent for basic studies on HCV virion assembly and entry, this monoclonal antibody should be useful for optimizing production and isolation of native HCV glycoprotein complexes for serodiagnostic and vaccine applications.
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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.