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Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1.
De La Cruz-Herrera, Carlos F; Tatham, Michael H; Siddiqi, Umama Z; Shire, Kathy; Marcon, Edyta; Greenblatt, Jack F; Hay, Ronald T; Frappier, Lori.
Afiliación
  • De La Cruz-Herrera CF; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
  • Tatham MH; Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
  • Siddiqi UZ; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
  • Shire K; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
  • Marcon E; Donnelly Centre, University of Toronto, Toronto, Canada.
  • Greenblatt JF; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
  • Hay RT; Donnelly Centre, University of Toronto, Toronto, Canada.
  • Frappier L; Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
PLoS Pathog ; 19(7): e1011477, 2023 07.
Article en En | MEDLINE | ID: mdl-37410772
SUMO modifications regulate the function of many proteins and are important in controlling herpesvirus infections. We performed a site-specific proteomic analysis of SUMO1- and SUMO2-modified proteins in Epstein-Barr virus (EBV) latent and lytic infection to identify proteins that change in SUMO modification status in response to EBV reactivation. Major changes were identified in all three components of the TRIM24/TRIM28/TRIM33 complex, with TRIM24 being rapidly degraded and TRIM33 being phosphorylated and SUMOylated in response to EBV lytic infection. Further experiments revealed TRIM24 and TRIM33 repress expression of the EBV BZLF1 lytic switch gene, suppressing EBV reactivation. However, BZLF1 was shown to interact with TRIM24 and TRIM33, resulting in disruption of TRIM24/TRIM28/TRIM33 complexes, degradation of TRIM24 and modification followed by degradation of TRIM33. Therefore, we have identified TRIM24 and TRIM33 as cellular antiviral defence factors against EBV lytic infection and established the mechanism by which BZLF1 disables this defence.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Infecciones por Virus de Epstein-Barr Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: PLoS Pathog Año: 2023 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Infecciones por Virus de Epstein-Barr Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: PLoS Pathog Año: 2023 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos