Structural Polypeptides of the Granulosis Virus of Plodia interpunctella†
AUTOR(ES)
Tweeten, Kathleen A.
RESUMO
Techniques were developed for the isolation and purification of three structural components of Plodia interpunctella granulosis virus: granulin, enveloped nucleocapsids, and nucleocapsids. The polypeptide composition and distribution of protein in each viral component were determined by sodium dodecyl sulfate discontinuous and gradient polyacrylamide slab gel electrophoresis. Enveloped nucleocapsids consisted of 15 structural proteins ranging in molecular weight from 12,600 to 97,300. Five of these proteins, having approximate molecular weights of 17,800, 39,700, 42,400, 48,200, and 97,300, were identified as envelope proteins by surface radioiodination of the enveloped nucleocapsids. Present in purified nucleocapsids were eight polypeptides. The predominant proteins in this structural component had molecular weights of 12,500 and 31,000. Whereas no evidence of polypeptide glycosylation was obtained, six of the viral proteins were observed to be phosphorylated.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=288613Documentos Relacionados
- Evidence for zinc binding by two structural proteins of Plodia interpunctella granulosis virus.
- Two-Dimensional Polyacrylamide Gel Analysis of Plodia interpunctella Granulosis Virus †
- Characterization of an alkaline protease associated with a granulosis virus of Plodia interpunctella.
- Isolation and purification of a granulosis virus from infected larvae of the Indian meal moth, Plodia interpunctella.
- Inhibitors of calling behavior of Plodia interpunctella
