ArticleJournal of virology2006
Functional analysis of hepatitis C virus envelope proteins, using a cell-cell fusion assay.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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
17 citing papers in PubMed, 44 citations in OpenAlex.
- Mathematical Modeling of Cell-Cell Fusion Assays to Characterize Virus-Mediated Cell Fusion.Advances in experimental medicine and biology · 2026Review
- Estimation of virus-mediated cell fusion rate of SARS-CoV-2.Virology · 2022Article
- A quantitative luciferase-based cell-cell fusion assay to measure four-serotype dengue virus E protein-triggered membrane fusion.Human vaccines & immunotherapeutics · 2020Article
- Tumor Microenvironment and Cell Fusion.BioMed research international · 2019Review
- The β-Lactamase Assay: Harnessing a FRET Biosensor to Analyse Viral Fusion Mechanisms.Sensors (Basel, Switzerland) · 2016Review
- Roles of lipoprotein receptors in the entry of hepatitis C virus.World journal of hepatology · 2015Review
- 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
- Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol.PloS one · 2011Article
- Enhancement of the influenza A hemagglutinin (HA)-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA).PloS one · 2009Article
- Low pH-dependent hepatitis C virus membrane fusion depends on E2 integrity, target lipid composition, and density of virus particles.The Journal of biological chemistry · 2009Article
- Lipids as modulators of membrane fusion mediated by viral fusion proteins.European biophysics journal : EBJ · 2007Review
- Studying hepatitis C virus: making the best of a bad virus.Journal of virology · 2007Review
- Characterization of fusion determinants points to the involvement of three discrete regions of both E1 and E2 glycoproteins in the membrane fusion process of hepatitis C virus.Journal of virology · 2007Article
- Biochemical mechanism of hepatitis C virus inhibition by the broad-spectrum antiviral arbidol.Biochemistry · 2007Article
- Transmembrane domains of hepatitis C virus envelope glycoproteins: residues involved in E1E2 heterodimerization and involvement of these domains in virus entry.Journal of virology · 2007Article
- Identification of conserved residues in the E2 envelope glycoprotein of the hepatitis C virus that are critical for CD81 binding.Journal of virology · 2006Article
- Arbidol: a broad-spectrum antiviral that inhibits acute and chronic HCV infection.Virology journal · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Hepatitis C virus (HCV) envelope proteins mediate the entry of virus into cells by binding to cellular receptors, resulting in fusion of the viral membrane with the host cell membrane and permitting the viral genome to enter the cytoplasm. We report the development of a robust and reproducible cell-cell fusion assay using envelope proteins from commonly occurring genotypes of HCV. The assay scored HCV envelope protein-mediated fusion by the production of fluorescent green syncytia and allowed us to elucidate many aspects of HCV fusion, including the pH of fusion, cell types that permit viral entry, and the conformation of envelope proteins essential for fusion. We found that fusion could be specifically inhibited by anti-HCV antibodies and by at least one peptide. We also generated a number of insertional mutations in the envelope proteins and tested nine of these using the fusion assay. We demonstrate that this fusion assay is a powerful tool for understanding the mechanism of HCV-mediated fusion, elucidating mutant function, and testing antiviral agents.
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Identifiers
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.