Analysis of the structural polypeptides of a porcine group C rotavirus.
AUTOR(ES)
Bremont, M
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=253325Documentos Relacionados
- Biochemical characterization of the structural and nonstructural polypeptides of a porcine group C rotavirus.
- Characterization of an antigenically distinct porcine rotavirus.
- VP4 serotype of the Gottfried strain of porcine rotavirus.
- Nucleotide sequences of genes 6 and 10 of a bovine group C rotavirus.
- Neutralizing monoclonal antibodies against three serotypes of porcine rotavirus.