VP5 autocleavage is required for efficient infection by in vitro-recoated aquareovirus particles.
J Gen Virol
; 96(Pt 7): 1795-800, 2015 Jul.
Article
en En
| MEDLINE
| ID: mdl-25742690
ABSTRACT
Grass carp reovirus (GCRV) is a member of the genus Aquareovirus in the family Reoviridae, and contains five core proteins (VP1-VP4 and VP6) and two outer-capsid proteins (VP5 and VP7) in its particle. Previous studies have revealed that the outer-capsid proteins of reovirus are responsible for initiating infection, but the mechanism is poorly understood. Using baculovirus-expressed VP5 and VP7 to recoat purified cores, in vitro assembly of GCRV was achieved in this study. Recoated GCRV (R-GCRV) closely resembled native GCRV (N-GCRV) in particle morphology, protein composition and infectivity. Similar to N-GCRV, the infectivity of R-GCRV could be inhibited by treating cells with the weak base NH4Cl. In addition, recoated particles carrying an AsnâAla substitution at residue 42 of VP5 (VP5N42A/VP7 R-GCRV) were no longer infectious. These results provide strong evidence that autocleavage of VP5 is critical for aquareovirus to initiate efficient infection.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Reoviridae
/
Proteínas Estructurales Virales
/
Internalización del Virus
Límite:
Animals
Idioma:
En
Revista:
J Gen Virol
Año:
2015
Tipo del documento:
Article