ArticleProceedings of the National Academy of Sciences of the United States of America2017
Mechanism of membrane fusion induced by vesicular stomatitis virus G protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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87 citing papers in PubMed, 138 citations in OpenAlex.
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- Low-density lipoproteins in human serum competitively inhibit the binding and entry of vesicular stomatitis virus.Molecular therapy. Advances · 2026Article
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- Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Development of a Live-Cell Imaging Assay to Elucidate Spatiotemporal Dynamics of Extracellular Vesicle Fusion with Target Cells.Journal of extracellular vesicles · 2026Article
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- Single-Virus Lipid-Mixing Study of Sendai Virus Provides Insight into Fusion Mechanism.ACS omega · 2025Article
- Engineering a streamlined virus-like particle for programmable tissue-specific gene delivery.Nature communications · 2025Article
- Bacterial Foreignization Nanosystem Elicits Multi-Phenotypic T Cells for Antitumor Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structures of vesicular stomatitis virus glycoprotein G alone and bound to a neutralizing antibody.PLoS pathogens · 2025Article
- Single VLP lipid-mixing measurements confirm off-pathway state in dengue virus fusion mechanism.Biophysical journal · 2025Article
- Unveiling the structural spectrum of SARS-CoV-2 fusion by in situ cryo-ET.Nature communications · 2025Article
27 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The glycoproteins (G proteins) of vesicular stomatitis virus (VSV) and related rhabdoviruses (e.g., rabies virus) mediate both cell attachment and membrane fusion. The reversibility of their fusogenic conformational transitions differentiates them from many other low-pH-induced viral fusion proteins. We report single-virion fusion experiments, using methods developed in previous publications to probe fusion of influenza and West Nile viruses. We show that a three-stage model fits VSV single-particle fusion kinetics: (i) reversible, pH-dependent, G-protein conformational change from the known prefusion conformation to an extended, monomeric intermediate; (ii) reversible trimerization and clustering of the G-protein fusion loops, leading to an extended intermediate that inserts the fusion loops into the target-cell membrane; and (iii) folding back of a cluster of extended trimers into their postfusion conformations, bringing together the viral and cellular membranes. From simulations of the kinetic data, we conclude that the critical number of G-protein trimers required to overcome membrane resistance is 3 to 5, within a contact zone between the virus and the target membrane of 30 to 50 trimers. This sequence of conformational events is similar to those shown to describe fusion by influenza virus hemagglutinin (a "class I" fusogen) and West Nile virus envelope protein ("class II"). Our study of VSV now extends this description to "class III" viral fusion proteins, showing that reversibility of the low-pH-induced transition and architectural differences in the fusion proteins themselves do not change the basic mechanism by which they catalyze membrane fusion.
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