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. 1988 Jun;62(6):2183–2185. doi: 10.1128/jvi.62.6.2183-2185.1988

Analysis of the structural polypeptides of a porcine group C rotavirus.

M Bremont 1, J Cohen 1, M A McCrae 1
PMCID: PMC253325  PMID: 2835518

Abstract

Polyacrylamide gel analysis of the structural polypeptides of purified group C virions allowed six major proteins to be identified. Of these, two (52,000- and 39,000-molecular-weight polypeptides) were shown to be in the outer virion shell as judged by the ability to strip them from virions by treatment with EDTA. Treatment of purified particles with endo-beta-N-acetylglucosaminidase F showed that the 39,000-molecular-weight outer shell polypeptide is probably posttranslationally glycosylated. Serological cross-comparison of groups A and C by using Western blotting (immunoblotting) extended the previously demonstrated lack of cross-reaction for the group antigen to show that none of the structural polypeptides cross-reacted. Possible implications of these findings for the epidemiology of rotaviruses are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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