Acid-Activated Structural Reorganization of the Rift Valley Fever Virus Gc Fusion Protein |
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| Authors: | S. M. de Boer J. Kortekaas L. Spel P. J. M. Rottier R. J. M. Moormann B. J. Bosch |
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| Affiliation: | aDepartment of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands;bCentral Veterinary Institute of Wageningen University and Research Centre, Department of Virology, Lelystad, The Netherlands |
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| 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 (
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