Cited 46 times since 1995 (1.6 per year) source: EuropePMC Journal of virology, Volume 69, Issue 8, 1 1 1995, Pages 4668-4674 The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers. de Vries AA, Post SM, Raamsman MJ, Horzinek MC, Rottier PJ
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.
