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dc.contributor.authorKim, Irene
dc.contributor.authorJenni, Simon
dc.contributor.authorStanifer, Megan
dc.contributor.authorRoth, Eatai
dc.contributor.authorWhelan, Sean
dc.contributor.authorvan Oijen, Antoine M.
dc.contributor.authorHarrison, Stephen
dc.date.accessioned2019-10-05T16:05:20Z
dc.date.issued2017
dc.identifier.citationKim, Irene S., Simon Jenni, Megan L. Stanifer, Eatai Roth, Sean P. J. Whelan, Antoine M. van Oijen, and Stephen C. Harrison. 2016. “Mechanism of Membrane Fusion Induced by Vesicular Stomatitis Virus G Protein.” Proceedings of the National Academy of Sciences 114 (1): E28–36. https://doi.org/10.1073/pnas.1618883114.
dc.identifier.issn0027-8424
dc.identifier.issn0744-2831
dc.identifier.issn1091-6490
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41483508*
dc.description.abstractThe 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.
dc.language.isoen_US
dc.publisherNational Academy of Sciences
dash.licenseLAA
dc.titleMechanism of membrane fusion induced by vesicular stomatitis virus G protein
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalProceedings of the National Academy of Sciences of the United States of America
dash.depositing.authorWhelan, Sean P. J.::1a236a1a655b3211832baaaf7e0e7860::600
dc.date.available2019-10-05T16:05:20Z
dash.workflow.comments1Science Serial ID 92778
dc.identifier.doi10.1073/pnas.1618883114
dash.source.volume114;1
dash.source.pageE28


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