Varicella-zoster virus gpI and herpes simplex virus gE: phosphorylation and Fc binding

gpI, the predominant varicella-zoster virus (VZV) envelope glycoprotein, was shown to be phosphorylated exclusively on serine and threonine residues, and phosphorylated gpI was detected in isolated virions. In cells infected with herpes simplex virus type 1 (HSV-1), a related neurotropic alpha-herpesvirus, HSV gE, the homolog to VZV gpI, and HSV gB, the homolog to VZV gpII, were also phosphorylated. The phosphate on gB and gE was alkali labile and resistant to endo H, suggesting linkage to serine and/or threonine. Although VZV gpI and HSV gE share sequence homology and similar post-translational modifications, no Fc-binding activity similar to that associated with gE was detected for gpI or any of the VZV glycoproteins.