The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers.
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.
de Vries
A A
AA
Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, The Netherlands.
Post
S M
SM
Raamsman
M J
MJ
Horzinek
M C
MC
Rottier
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers; D002415:Cats; D002460:Cell Line; D006224:Cricetinae; D004220:Disulfides / Q000737:chemistry*; D007240:Equartevirus / Q000737:chemistry*; D007700:Kinetics; D008969:Molecular Sequence Data; D019814:Myristic Acid; D009227:Myristic Acids / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000378:metabolism; D014771:Virion / Q000737:chemistry / Q000378:metabolism
D001704:Biopolymers; D004220:Disulfides; D009227:Myristic Acids; D014759:Viral Envelope Proteins; D014763:Viral Matrix Proteins; D019814:Myristic Acid