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 s 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--acetylglucosaminidase H (endo H) and endo-β--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 -linked oligosaccharides, whereas those of gp65 and gp63 are complex type -linked oligosaccharides.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error