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Proteomic analysis of ubiquitin-like posttranslational modifications induced by the adenovirus E4-ORF3 protein.


ABSTRACT:

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Viruses interact with and regulate many host metabolic pathways in order to advance the viral life cycle and counteract intrinsic and extrinsic antiviral responses. The human adenovirus (Ad) early protein E4-ORF3 forms a unique scaffold throughout the nuclei of infected cells and inhibits multiple antiviral defenses, including a DNA damage response (DDR) and an interferon response. We previously reported that the Ad5 E4-ORF3 protein induces sumoylation of Mre11 and Nbs1, which are essential for the DDR, and their relocalization into E4-ORF3-induced nuclear inclusions is required for this modification to occur. In this study, we sought to analyze a global change in ubiquitin-like (Ubl) modifications, with particular focus on SUMO3, by the Ad5 E4-ORF3 protein and to identi

SUBMITTER: Sohn SY 

PROVIDER: S-EPMC4300750 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature