Open AccessViral manipulation of cellular protein conjugation pathways: The SUMO lesson
Author(s) -
Domenico Mattoscio,
Chiara V. Segré,
Susanna Chiocca
Publication year - 2013
Publication title -
world journal of virology
Language(s) - English
Resource type - Journals
ISSN - 2220-3249
DOI - 10.5501/wjv.v2.i2.79
Subject(s) - sumo protein , viral replication , function (biology) , ubiquitin , microbiology and biotechnology , biology , mechanism (biology) , evasion (ethics) , posttranslational modification , immune system , viral infection , computational biology , replication (statistics) , virus , virology , immunology , genetics , biochemistry , gene , philosophy , epistemology , enzyme
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.