@article{mbs:/content/journal/jgv/10.1099/0022-1317-68-10-2587, author = "Sullivan, Veronica and Smith, Geoffrey L.", title = "Expression and Characterization of Herpes Simplex Virus Type 1 (HSV-1) Glycoprotein G (gG) by Recombinant Vaccinia Virus: Neutralization of HSV-1 Infectivity with Anti-gG Antibody", journal= "Journal of General Virology", year = "1987", volume = "68", number = "10", pages = "2587-2598", doi = "https://doi.org/10.1099/0022-1317-68-10-2587", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-68-10-2587", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "recombinant vaccinia virus", keywords = "HSV-1", keywords = "gG", abstract = "SUMMARY 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.", }