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Reversible Acid-Induced Inactivation of the Membrane Fusion Protein of Semliki Forest Virus

By Barry-Lee Waarts, Jolanda M. Smit, Onwuchekwa J. C. Aneke, Gerald M. McInerney, Peter Liljeström, Robert Bittman and Jan Wilschut

Abstract

Previously, it has been shown that the exposure of Semliki Forest virus (SFV) to a mildly acidic environment induces a rapid and complete loss of the ability of the virus to bind and fuse to target membranes added subsequently. In the present study, incubation of SFV at low pH followed by a specific reneutralization step resulted in a partial reversion of this loss of viral fusion capacity, as assessed in a liposomal model system. Also, the ability of the viral E1 fusion protein to undergo liposome-stimulated trimerization was restored. Furthermore, acid-treated and neutralized SFV largely retained infectivity. Exposure of SFV to low pH induced dissociation of the E1/E2 heterodimer, which was not reversed upon neutralization. It is concluded that the SFV E1 fusion protein, after acid-induced dissociation from E2, rapidly adopts an intermediate, nontrimeric conformation in which it is no longer able to interact with target membrane lipids. Neutralization restores the ability of E1 to interact with membranes. This interaction, however, remains strictly dependent on low pH

Topics: Structure and Assembly
Publisher: American Society for Microbiology
Year: 2005
DOI identifier: 10.1128/JVI.79.12.7942-7948.2005
OAI identifier: oai:pubmedcentral.nih.gov:1143635
Provided by: PubMed Central
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