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pubmed-article:1711988pubmed:abstractTextBovine rotavirus proteins were analysed by a panel of monoclonal antibodies. Glycosylated epitopes were identified on both inner and outer capsid proteins (VP6 and VP7 respectively). VP7 possessed a periodate insensitive epitope which was, however, sensitive to endoglycosidase H, mixed glycosidases and to protease treatment. This epitope was not detected on viruses grown in the presence of 2-deoxy-D-glucose or tunicamycin. An epitope was detected on VP6 which was sensitive to periodate oxidation. The blotted protein reacted with a glycan assay kit; yet the epitope was not affected by endoglycosidase H and was found on viruses grown in the presence of 2-deoxy-D-glucose or tunicamycin. These results suggest that VP7 and VP6 epitopes are carbohydrate dependent. The VP7 epitope contains an N-linked carbohydrate moiety in contrast to the VP6 epitope which appears to contain O-linked glycosyl units.lld:pubmed
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pubmed-article:1711988pubmed:articleTitleCharacterization of bovine rotavirus VP6 and VP7 as glycoproteins using monoclonal antibodies.lld:pubmed
pubmed-article:1711988pubmed:affiliationVirology Section, Faculty of Veterinary Medicine, University of Montreal, Quebec, Canada.lld:pubmed
pubmed-article:1711988pubmed:publicationTypeJournal Articlelld:pubmed