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Acid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein.

ABSTRACT: The entry of the enveloped Rift Valley fever virus (RVFV) into its host cell is mediated by the viral glycoproteins Gn and Gc. We investigated the RVFV entry process and, in particular, its pH-dependent activation mechanism using our recently developed nonspreading-RVFV-particle system. Entry of the virus into the host cell was efficiently inhibited by lysosomotropic agents that prevent endosomal acidification and by compounds that interfere with dynamin- and clathrin-dependent endocytosis. Exposure of plasma membrane-bound virions to an acidic pH (

SUBMITTER: de Boer SM

PROVIDER: S-EPMC3503025 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Acid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein.

de Boer S M SM Kortekaas J J Spel L L Rottier P J M PJ Moormann R J M RJ Bosch B J BJ

Journal of virology 20121003 24

The entry of the enveloped Rift Valley fever virus (RVFV) into its host cell is mediated by the viral glycoproteins Gn and Gc. We investigated the RVFV entry process and, in particular, its pH-dependent activation mechanism using our recently developed nonspreading-RVFV-particle system. Entry of the virus into the host cell was efficiently inhibited by lysosomotropic agents that prevent endosomal acidification and by compounds that interfere with dynamin- and clathrin-dependent endocytosis. Expo ...[more]

PMID: 23035232

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