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. 1995 Aug;69(8):4668–4674. doi: 10.1128/jvi.69.8.4668-4674.1995

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

A A de Vries 1, S M Post 1, M J Raamsman 1, M C Horzinek 1, P J Rottier 1
PMCID: PMC189270  PMID: 7609031

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.

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Selected References

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