Assembly and organization of glycoproteins B, C, D, and H in herpes simplex virus type 1 particles lacking individual glycoproteins: No evidence for the formation of a complex of these molecules

Glycoprotein B (gB), gC, go, and gH:L of herpes simplex virus type 1 (HSV-1 ) are implicated in virus adsorption and penetration. gB, go, and gH:L are essential for these processes, and their expression is necessary and suffic ient to induce cell fusion. The current view is that these molecules act in concert as a functional complex, and cross-linking studies support this vi ew (C. G. Handler, R. J, Eisenberg, and G. H. Cohen, J. Virol. 70:6067-6075 , 1996). We examined the glycoprotein composition, with respect to gB, gC, go, and gB, of mutant virions lacking individual glycoproteins and the sedi mentation characteristics of glycoproteins extracted from these virions. Th e amounts of gB, gC, go, or gH detected in virions did not alter, when any one of these molecules was absent, and it therefore appears that they are i ncorporated into the virion independently of each other. The sedimentation characteristics of gB and go from mutant virions were not different from th ose of wild-type virions. We confirmed that gB, gC, and go could be cross-l inked to each other on the virion surface but found that the absence of one glycoprotein did not alter the outcome of cross-linking reactions between the remaining molecules. The incorporation and arrangement of these glycopr oteins in the virion envelope therefore appear to be independent of the ind ividual molecular species. This is difficult to reconcile with the concept that gB, gC, go, and gH:L are incorporated as a functional complex into the virion envelope.