Further biochemical characterization, including the detection of surface glycoproteins, of human, calf, and simian rotaviruses.
Polyacrylamide gel electrophoretic analysis of purified preparation of the simian rotavirus SA-11 indicated eight polypeptide components that migrated in a manner remarkably similar to those of the previously characterized human and calf rotaviruses. Analyses of preparations of single-shelled and double-shelled particles of human, calf, and simian an rotaviruses have also permitted assignment of the polypeptides to the inner or outer shells. The major components of the outer shells of each virus have been identified as glycoproteins, and the importance of this in terms of host cell specificity is discussed. Sensitivities of the various rotaviruses to acid, proteases, and glycosidases were also investigated.
D000818:Animals; D002417:Cattle; D005696:Galactosidases / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis*; D000882:Haplorhini; D006801:Humans; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000032:analysis; D012328:RNA Viruses / Q000032:analysis*; D012401:Rotavirus / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D014764:Viral Proteins / Q000032:analysis*; D001616:beta-Galactosidase / Q000378:metabolism
D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins; D005696:Galactosidases; D001616:beta-Galactosidase; D010447:Peptide Hydrolases