@article{mbs:/content/journal/jgv/10.1099/0022-1317-73-7-1693, author = "Qin, Ke-feng and Yu, Qi-gui and Gao, Qian and Wang, Mei-xian and Jiang, Shao-zhun", title = "Identification and characterization of a 30K glycoprotein of herpes simplex virus type 2", journal= "Journal of General Virology", year = "1992", volume = "73", number = "7", pages = "1693-1701", doi = "https://doi.org/10.1099/0022-1317-73-7-1693", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-73-7-1693", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "A herpes simplex virus type 2 (HSV-2) type-specific monoclonal antibody (MAb), CH-A9, precipitated a glycoprotein with an M r of approximately 30000 (g30K) from extracts of HSV-2-infected BHK cells labelled with [3H]leucine, [14C]fructose or [3H]glucosamine. The M r of this glycoprotein is lower than those of other HSV glycoproteins. Immunoassays of BHK cells infected with HSV-1-HSV-2 intertypic recombinants localized the gene encoding the target antigen of MAb CH-A9 to the unique long (UL) region at map units 0.490 to 0.564. Tunicamycin effectively inhibits N-linked glycosylation of g30K, which suggests that g30K may be modified by addition of N-linked oligosaccharides and that the amino acid sequence may contain Asn-X-Ser or Asn-X-Thr. The g30K was also purified on an immunoadsorbent column consisting of MAb CH-A9 linked to Sepharose 4B and was shown to be an HSV-2 type-specific antigen by indirect ELISA. The glycoprotein could induce HSV-2 type-specific neutralizing antibody in BALB/c mice. This evidence suggests that g30K may be a novel glycoprotein of HSV-2.", }