Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways

Viruses

Peter Wimmer¹  Sabrina Schreiner² 

[1] Novartis Pharma Germany, Roonstrasse 25, 90429 Nürnberg, Germany;;Institute of Virology, Technische Universität München, Trogerstrasse 30, 81675 München, Germany

关键词: SUMO;    ubiquitin;    virus;    analogue;    mimicry;    SENP;    DUB;   

DOI  :  10.3390/v7092849

来源: mdpi

【 摘 要 】

Posttranslational modifications (PTMs) of proteins include enzymatic changes by covalent addition of cellular regulatory determinants such as ubiquitin (Ub) and small ubiquitin-like modifier (SUMO) moieties. These modifications are widely used by eukaryotic cells to control the functional repertoire of proteins. Over the last decade, it became apparent that the repertoire of ubiquitiylation and SUMOylation regulating various biological functions is not restricted to eukaryotic cells, but is also a feature of human virus families, used to extensively exploit complex host-cell networks and homeostasis. Intriguingly, besides binding to host SUMO/Ub control proteins and interfering with the respective enzymatic cascade, many viral proteins mimic key regulatory factors to usurp this host machinery and promote efficient viral outcomes. Advanced detection methods and functional studies of ubiquitiylation and SUMOylation during virus-host interplay have revealed that human viruses have evolved a large arsenal of strategies to exploit these specific PTM processes. In this review, we highlight the known viral analogs orchestrating ubiquitin and SUMO conjugation events to subvert and utilize basic enzymatic pathways.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.