Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein

HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP...

Descripción completa

Detalles Bibliográficos
Autores principales: Wang, Lei, Liu, Longding, Che, Yanchun, Wang, Lichun, Jiang, Li, Dong, Chenghong, Zhang, Ying, Li, Qihan
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Research
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2913958/
https://www.ncbi.nlm.nih.gov/pubmed/20630051
http://dx.doi.org/10.1186/1743-422X-7-156
Descripción
Sumario:HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally, analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

Ejemplares similares