Abstract
A recombinant vaccinia virus expressing herpes simplex virus type 1 (HSV-1) glycoprotein G (gG) has been constructed. Cells infected with this recombinant virus (gG-VAC) synthesized glycosylated proteins of 48K, 57K and 61K mol. wt. that were recognized by anti-HSV-1 sera. Rabbits and mice vaccinated with the live recombinant virus produced antibodies that recognized 48K, 57K and 61K mol. wt. proteins in HSV-1-infected cells. The gG polypeptides were present on cytoplasmic and nuclear membranes during infection with both HSV-1 and recombinant vaccinia virus gG-VAC. The 57K and 61K mol. wt. gG polypeptides were present in purified HSV-1 virions and were targets for antibody-mediated complement-dependent virus neutralization.