@article{mbs:/content/journal/jgv/10.1099/0022-1317-74-3-495, author = "Ellinger, K. and Neipel, F. and FoĆ -Tomasi, L. and Campadelli-Fiume, G. and Fleckenstein, B.", title = "The glycoprotein B homologue of human herpesvirus 6", journal= "Journal of General Virology", year = "1993", volume = "74", number = "3", pages = "495-500", doi = "https://doi.org/10.1099/0022-1317-74-3-495", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-74-3-495", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The gene for the homologue of herpesvirus glycoprotein B (gB) has been identified in the genome of human herpesvirus 6 (HHV-6), strain U1102, and the nucleotide sequence was determined. The open reading frame encodes a protein of 830 amino acids (93.2K) with the characteristics of a transmembrane glycoprotein and close similarity to the gp58/116 complex of human cytomegalovirus (HCMV). Monoclonal antibodies 2D10 and 2B9 have been shown previously to react with an HHV-6 glycoprotein of apparent M r 112K, and its proteolytic cleavage products of M r 64K and 58K. We show that both monoclonal antibodies detect prokaryotically expressed carboxy-terminal fragments of the HHV-6 gB homologue. This indicates that the HHV-6 gB homologue is probably processed by proteolytic cleavage similar to its equivalents in HCMV and various other herpesviruses.", }