Regulation of vaccinia virus E3 protein by small ubiquitin-like modifier proteins

The vaccinia virus (VACV) E3 protein is essential for virulence and has antiapoptotic activity and the ability to impair the host innate immune response. Here we demonstrate that E3 interacts with SUMO1 through a small ubiquitin-like modifier (SUMO)-interacting motif (SIM). SIM integrity is required...

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Detalles Bibliográficos
Autores: González-Santamaría, José, Campagna, Michela, García, Maria Angel, Marcos-Villar, Laura, González, Dolores, Gallego, Pedro, Lopitz-Otsoa, Fernando, Guerra García, María Susana, Rodríguez, Manuel S., Estéban, Mariano R., Rivas, Carmen
Tipo de recurso: artículo
Fecha de publicación:2011
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/664899
Acceso en línea:http://hdl.handle.net/10486/664899
https://dx.doi.org/10.1128/JVI.05628-11
Access Level:acceso abierto
Palabra clave:Vaccinia virus
Medicina
Descripción
Sumario:The vaccinia virus (VACV) E3 protein is essential for virulence and has antiapoptotic activity and the ability to impair the host innate immune response. Here we demonstrate that E3 interacts with SUMO1 through a small ubiquitin-like modifier (SUMO)-interacting motif (SIM). SIM integrity is required for maintaining the stability of the viral protein and for the covalent conjugation of E3 to SUMO1 or SUMO2, a modification that has a negative effect on the E3 transcriptional transactivation of the p53-upregulated modulator of apoptosis (PUMA) and APAF-1 genes. We also demonstrate that E3 is ubiquitinated, a modification that does not destabilize the wild-type protein but triggers the degradation of an E3- SIM mutant. This report constitutes the first demonstration of the important roles that both SUMO and ubiquitin play in the regulation of the VACV protein E3

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