SUMMARYThe structural glycoproteins of calf (BDV 486), human (Wa) and Simian (SAIl) rotaviruses were compared for sensitivity to endoglycosidase (Endo) H. The calf and human virus glycoproteins were reduced by approximately 5000 molecular weight in two equal stages. The simian rotavirus glycoprotein sustained only one 2500 molecular weight decrease. The effect of the host cell on the viral oligosaccharide composition was examined. Endo H digests of calf rotavirus 82-124 extracted from stool and its progeny propagated and [35S]methionine-labelled in MA104 cells were compared. Endo H had the same effects on the glycoproteins, indicating that the nature of the host cell does not affect the oligosaccharide composition of the virus glycoproteins.

SUMMARYThe oligosaccharides of the structural glycoprotein (VP7)of calf rotavirus were characterized. The precursor of VP7 produced in infected cells in the presence of tunicamycin migrated on SDS-polyacrylamide gels with an apparent molecular weight 6000 less than the glycosylated glycoprotein. Endoglycosidase (Endo) H digestion of the mature virus resulted in a decrease of 5000 in the molecular weight of VP7 in two discrete stages. Analysis of Endo H-treated, 3H-labelled digestion products of VP7 on Bio-Gel P-4 identified an oligosaccharide of molecular weight 1350 as the predominant form. Further treatment of the digest with mannosidase and analysis on Bio-Gel P-2 columns indicated that the oligosaccharide was digested into a free mannose and an oligosaccharide of molecular weight 400 in the ratio of 6:1. This indicates that the oligosaccharides of VP7 consist of four N-linked (Man)7 residues, two of which occupy more exposed and two more cryptic positions in the VP7 molecule.