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World J Virol. May 12, 2013; 2(2): 79-90
Published online May 12, 2013. doi: 10.5501/wjv.v2.i2.79
Viral manipulation of cellular protein conjugation pathways: The SUMO lesson
Domenico Mattoscio, Chiara V Segré, Susanna Chiocca
Domenico Mattoscio, Chiara V Segré, Susanna Chiocca, Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy
Author contributions: Mattoscio D, Segré CV and Chiocca S wrote the paper.
Correspondence to: Susanna Chiocca, PhD, Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, 20139 Milan, Italy. susanna.chiocca@ieo.eu
Telephone: +39-2-57489835 Fax: +39-2-94375990
Received: December 5, 2012
Revised: January 23, 2013
Accepted: February 5, 2013
Published online: May 12, 2013
Abstract

Small ubiquitin-like modifier (SUMO)ylation is a key post-translational modification mechanism that controls the function of a plethora of proteins and biological processes. Given its central regulatory role, it is not surprising that it is widely exploited by viruses. A number of viral proteins are known to modify and/or be modified by the SUMOylation system to exert their function, to create a cellular environment more favorable for virus survival and propagation, and to prevent host antiviral responses. Since the SUMO pathway is a multi-step cascade, viral proteins engage with it at many levels, to advance and favor each stage of a typical infection cycle: replication, viral assembly and immune evasion. Here we review the current knowledge on the interplay between the host SUMO system and viral lifecycle.

Keywords: Virus, Small ubiquitin-like modifier, Small ubiquitin-like modifier-ylation, Exploitation, Virus assembly, Immune evasion, Innate immunity