@article{mbs:/content/journal/jgv/10.1099/0022-1317-66-2-231, author = "Snowden, B. Wendy and Kinchington, Paul R. and Powell, Kenneth L. and Halliburton, Ian W.", title = "Antigenic and Biochemical Analysis of gB of Herpes Simplex Virus Type 1 and Type 2 and of Cross-reacting Glycoproteins Induced by Bovine Mammillitis Virus and Equine Herpesvirus Type 1", journal= "Journal of General Virology", year = "1985", volume = "66", number = "2", pages = "231-247", doi = "https://doi.org/10.1099/0022-1317-66-2-231", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-66-2-231", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "gB", keywords = "tryptic peptide analysis", keywords = "herpesvirus", keywords = "common antigen", abstract = "SUMMARY An antiserum was produced to the oligomeric form of glycoprotein B (gB) induced by herpes simplex virus type 1 (HSV-1) strain 17. This antiserum gave a single common precipitin line in agar gel immunodiffusion with HSV-1, HSV-2, bovine mammillitis virus (BMV) and equine herpesvirus type 1 (EHV-1). It also neutralized HSV-1, HSV-2 and BMV but not EHV-1. Absorption of the antiserum with excess HSV-2 or BMV antigen resulted in an HSV-1-specific neutralizing antiserum. In immunoprecipitation, two proteins, gB and pgB, were precipitated from HSV-1- and HSV-2-infected cells and at least three from BMV- and EHV-1-infected cells. Glycoprotein B and pgB of three HSV-1 and three HSV-2 strains and the corresponding antigenically related glycoproteins of BMV- and EHV-1-infected cells were labelled with 125I, digested with trypsin and the resulting peptides separated by two-dimensional thin-layer chromatography or high-pressure liquid chromatography. The resulting profiles were found to be almost identical, suggesting considerable structural conservation of the peptide backbone of the antigenically related glycoproteins of these four viruses.", }