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Viruses 2010, 2(10), 2356-2380;

Poxvirus Exploitation of the Ubiquitin-Proteasome System

Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, T6G 2S2, Canada
Author to whom correspondence should be addressed.
Received: 2 September 2010 / Revised: 27 September 2010 / Accepted: 30 September 2010 / Published: 19 October 2010
(This article belongs to the Special Issue Viruses and the Ubiquitin/Proteasome System)
PDF [549 KB, uploaded 12 May 2015]


Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been shown to encode BTB/kelch and ankyrin/F-box proteins that interact with cullin-3 and cullin-1 based ubiquitin ligases, respectively. Multiple members of the poxvirus family also encode ubiquitin ligases with intrinsic activity. This review describes the numerous mechanisms that poxviruses employ to manipulate the ubiquitin-proteasome system.
Keywords: poxvirus; ubiquitin; F-box; BTB/kelch; RING finge poxvirus; ubiquitin; F-box; BTB/kelch; RING finge
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Barry, M.; Van Buuren, N.; Burles, K.; Mottet, K.; Wang, Q.; Teale, A. Poxvirus Exploitation of the Ubiquitin-Proteasome System. Viruses 2010, 2, 2356-2380.

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