Association of reovirus outer capsid proteins sigma 3 and mu 1 causes a conformational change that renders sigma 3 protease sensitive.
J Virol
; 69(12): 8180-4, 1995 Dec.
Article
em En
| MEDLINE
| ID: mdl-7494347
ABSTRACT
Association of the reovirus proteins sigma 3 and mu 1 influences viral entry, initiation of outer capsid assembly, and modulation of the effect of sigma 3 on cellular translation. In this study, we have addressed whether structural changes occur in sigma 3 as a result of its interaction with mu 1. Using differences in protease sensitivity to detect conformationally distinct forms of sigma 3, we showed that association of sigma 3 with mu 1 caused a conformational change in sigma 3 that converted it from a protease-resistant to a protease-sensitive structure and occurred posttranslationally. The effect of mu 1 on the structure of sigma 3 was stoichiometric. Our results are consistent with a model in which sigma 3's association with mu 1 shifts its function from translational control to assembly of an outer capsid in which sigma 3 is folded into the protease-sensitive conformation that is required for its cleavage during the next round of infection.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Reoviridae
/
Proteínas Virais
/
Serina Endopeptidases
/
Capsídeo
/
Proteínas de Ligação a RNA
/
Proteínas do Capsídeo
Tipo de estudo:
Diagnostic_studies
/
Etiology_studies
/
Risk_factors_studies
Limite:
Animals
Idioma:
En
Revista:
J Virol
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Estados Unidos