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

Autor: Horzinek, M.C., Vries, A.A. de, Post, S.M., Raamsman, M.J., Rottier, P.J.M.
Jazyk: angličtina
Rok vydání: 1995
Předmět:
Zdroj: Journal of virology, 69(8), 4668. American Society for Microbiology
ISSN: 0022-538X
Popis: 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.
Databáze: OpenAIRE