Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.
Virology
; 489: 223-32, 2016 Feb.
Article
en En
| MEDLINE
| ID: mdl-26773383
ABSTRACT
The Epstein-Barr virus glycoprotein complex gMgN has been implicated in assembly and release of fully enveloped virus, although the precise role that it plays has not been elucidated. We report here that the long predicted cytoplasmic tail of gM is not required for complex formation and that it interacts with the cellular protein p32, which has been reported to be involved in nuclear egress of human cytomegalovirus and herpes simplex virus. Although redistribution of p32 and colocalization with gM was not observed in virus infected cells, knockdown of p32 expression by siRNA or lentivirus-delivered shRNA recapitulated the phenotype of a virus lacking expression of gNgM. A proportion of virus released from cells sedimented with characteristics of virus lacking an intact envelope and there was an increase in virus trapped in nuclear condensed chromatin. The observations suggest the possibility that p32 may also be involved in nuclear egress of Epstein-Barr virus.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas del Envoltorio Viral
/
Herpesvirus Humano 4
/
Infecciones por Virus de Epstein-Barr
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Virology
Año:
2016
Tipo del documento:
Article
País de afiliación:
Estados Unidos