Distinct glycoprotein O complexes arise in a post-Golgi compartment of cytomegalovirus-infected cells.

Human cytomegalovirus (CMV) glycoproteins H, L, and O (gH, gL, and gO, respectively) form a heterotrimeric disulfide-bonded complex that participates in the fusion of the viral envelope with the host cell membrane. During virus maturation, this complex undergoes a series of intracellular assembly and processing events which are not entirely defined (M. T. Huber and T. Compton, J. Virol. 73:3886-3892, 1999). Here, we demonstrate that gO does not undergo the same posttranslational processing in transfected cells as it does in infected cells. We further determined that gO is modified by O-linked glycosylation and that this terminally processed form is highly enriched in virions. However, during studies of gO processing, novel gO complexes were discovered in CMV virions. The newly identified gO complexes, including gO-gL heterodimers, were not readily detected in CMV-infected cells. Further characterization of the trafficking of gO through the secretory pathway of infected cells localized gH, gL, and gO primarily to the Golgi apparatus and trans-Golgi network, supporting the conclusion that the novel virion-associated gO complexes arise in a post-Golgi compartment of infected cells.