Equine herpesvirus-4 glycoprotein G is secreted as a disulphide-linked homodimer and is present as two homodimeric species in the virion

Abstract

Glycoprotein G (gG) homologues have been found in most alphaherpesviruses although little is known about their structure or function. In this study, three species of equine herpesvirus-4 (EHV-4) gG were identified: a full-length 68 kDa virion-associated species (gGV(L)), a 12 kDa virion-associated species (gGV,) and a 60 kDa secreted species (gGS), detected in the medium of infected cells, gGS and gGV(S) appear to be proteolytic cleavage products of gGV(L) and correspond to the N- and C-terminal regions, respectively. It was shown that gGS and gGV(L) are similarly glycosylated possessing mostly N-linked complex-type carbohydrate side chains. Western blots of proteins separated under nonreduc..