RT Journal Article SR Electronic(1) A1 Okuno, Toshiomi A1 Shao, Hui A1 Asada, Hideo A1 Shiraki, Kimiyasu A1 Takahashi, Michiaki A1 Yamanishi, KoichiYR 1992 T1 Analysis of human herpesvirus 6 glycoproteins recognized by monoclonal antibody OHV1 JF Journal of General Virology, VO 73 IS 2 SP 443 OP 447 DO https://doi.org/10.1099/0022-1317-73-2-443 PB Microbiology Society, SN 1465-2099, AB A virus-specific glycoprotein (gp) from human herpesvirus 6 (HHV-6) was studied using the anti-HHV-6 monoclonal antibody OHV1. Immunoprecipitation with extracts from infected cells revealed that the antibody recognized four glycosylated proteins (gps) with M rs of 106K, 102K, 65K and 63K under reducing conditions. However, only two gps, of 106K (gp106) and 102K, were detected under non-reducing conditions. Pulse-chase experiments revealed that gp65 and gp63 were cleavage products of gp106 and gp102. When infected cells were treated with tunicamycin, none of these gps was detected. With endo-β-N-acetylglucosaminidase H (endo H) and endo-β-N-acetylglucosaminidase F (endo F) treatment, gp106 and gp102 disappeared. Moreover, gp65 and gp63 were not affected by endo H treatment but were sensitive to endo F treatment. These data suggest that sugar residues of gp106 and gp102 are high-mannose type N-linked oligosaccharides, whereas those of gp65 and gp63 are complex type N-linked oligosaccharides., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-73-2-443