ArticleJournal of viral hepatitis2009
Mutational analysis of the hepatitis C virus E1 glycoprotein in retroviral pseudoparticles and cell-culture-derived H77/JFH1 chimeric infectious virus particles.
Article in Journal of viral hepatitis, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Hepatitis C virus E1 protein-specific linear B-cell epitopes, pan-genotype reactivity, and functional relevance.Frontiers in immunology · 2026Article
- A protein coevolution method uncovers critical features of the Hepatitis C Virus fusion mechanism.PLoS pathogens · 2018Article
- The Neutralizing Face of Hepatitis C Virus E2 Envelope Glycoprotein.Frontiers in immunology · 2018Review
- Evolutionary Analysis Provides Insight Into the Origin and Adaptation of HCV.Frontiers in microbiology · 2018Article
- Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.Frontiers in immunology · 2018Review
- The unexpected structures of hepatitis C virus envelope proteins.Experimental and therapeutic medicine · 2017Article
- A Biologically-validated HCV E1E2 Heterodimer Structural Model.Scientific reports · 2017Article
- Hepatitis C virus resistance to broadly neutralizing antibodies measured using replication-competent virus and pseudoparticles.The Journal of general virology · 2016Article
- Novel functional hepatitis C virus glycoprotein isolates identified using an optimized viral pseudotype entry assay.The Journal of general virology · 2016Article
- Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Journal of virology · 2015Article
- Review
- Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design.Current opinion in virology · 2015Review
- Unexpected structural features of the hepatitis C virus envelope protein 2 ectodomain.Journal of virology · 2014Review
- Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Viruses · 2014Review
- Comprehensive linker-scanning mutagenesis of the hepatitis C virus E1 and E2 envelope glycoproteins reveals new structure-function relationships.The Journal of general virology · 2011Article
- Review
- Identification of interactions in the E1E2 heterodimer of hepatitis C virus important for cell entry.The Journal of biological chemistry · 2011Article
- Identification of new functional regions in hepatitis C virus envelope glycoprotein E2.Journal of virology · 2011Article
- Antigen-specific proteolysis by hybrid antibodies containing promiscuous proteolytic light chains paired with an antigen-binding heavy chain.The Journal of biological chemistry · 2009Article
- Hepatitis C virus NS2 protein contributes to virus particle assembly via opposing epistatic interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes.Journal of virology · 2009Article
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 2 institutions in 2 countries.
Funding
Abstract
Cell entry by enveloped viruses is mediated by viral glycoproteins, and generally involves a short hydrophobic peptide (fusion peptide) that inserts into the cellular membrane. An internal hydrophobic domain within E1 (aa262-290) of hepatitis C virus (HCV) may function as a fusion peptide. Retrovirus-based HCV-pseudotyped viruses (HCVpp; genotype 1a) containing Ala or Pro substitutions at conserved amino acid positions within this putative fusion peptide were generated. Mutation of conserved residues significantly reduced efficiency of HCVpp entry into Huh-7 cells. The majority of amino acid substitutions appeared to disrupt necessary interactions between E1 and E2. For some mutants, reductions in HCVpp-associated E1 were associated with the incorporation of a high molecular weight, hyperglycosylated E2 that displayed decreased CD81-binding. Other entry-deficient mutants displayed normal E1E2 incorporation into pseudoparticles and normal CD81-binding, and therefore might affect viral fusion. One mutant (S283P) consistently displayed two- to threefold higher infectivity than did wild-type. Three mutations that decreased HCVpp infectivity also reduced levels of HCVcc infectious virus production. However, the S283P mutation had a different effect in the two systems as it did not increase production of infectious HCVcc. This comprehensive mutational analysis of the putative HCV fusion peptide provides insight into the role of E1 in its interaction with E2 and in HCV entry.
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What OpenQuestion holds
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.