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J. Virol., Aug 1995, 4668-4674, Vol 69, No. 8
Copyright © 1995, American Society for Microbiology

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

AA de Vries, SM Post, MJ Raamsman, MC Horzinek and PJ Rottier
Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, The Netherlands.

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.

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