The study demonstrates that the GL and M envelope proteins of equine arteritis virus form disulfide-linked heterodimers essential for incorporation into virus particles.
No immediate implications for equine arteritis management; leaves open whether GL-M heterodimers are required for infectivity across arteriviruses.
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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Vries et al. (1995) studied this question.
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