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The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers

By M.C. Horzinek, A.A. de Vries, S.M. Post, M.J. Raamsman and P.J.M. Rottier

Abstract

In a coimmunoprecipitation assay with monospecific antisera, the two major envelope proteins GL and M of equine arteritis virus were found to occur in heteromeric complexes in virions and infected cells. While the GL protein associated with M rapidly and efficiently, newly synthesized M protein was incorporated into complexes at a slower rate, which implies that it interacts with GL molecules synthesized earlier. Analysis under nonreducing conditions revealed that the GL/M complexes consist of disulfide-linked heterodimeric structures. Pulse-chase experiments showed that virtually all GL monomers ended up in heterodimers, whereas a fraction of the M protein persisted as monomers. The M protein also formed covalently linked homodimers, but only the heterodimers were incorporated into virus particles

Topics: Diergeneeskunde
Year: 1995
OAI identifier: oai:dspace.library.uu.nl:1874/3485
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