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

S.M. de Boer, J.A. Kortekaas, L. Spel, P.J.M. Rottier, R.J.M. Moormann, B.J. Bosch

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39 Citations (Scopus)

Abstract

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 its pH-dependent activation mechanism in particular 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 (
Original languageEnglish
Pages (from-to)13642-13652
JournalJournal of Virology
Volume86
Issue number24
DOIs
Publication statusPublished - 2012

Keywords

  • semliki-forest-virus
  • conserved histidine-residues
  • triggering membrane-fusion
  • cell-fusion
  • uukuniemi-virus
  • mediated endocytosis
  • hemorrhagic-fever
  • enveloped viruses
  • mammalian-cells
  • influenza-virus

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    de Boer, S. M., Kortekaas, J. A., Spel, L., Rottier, P. J. M., Moormann, R. J. M., & Bosch, B. J. (2012). Acid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein. Journal of Virology, 86(24), 13642-13652. https://doi.org/10.1128/JVI.01973-12