Interplay between poxviruses and the cellular ubiquitin/ubiquitin-like pathways

Abstract 

Post-translational polypeptide tagging by conjugation with ubiquitin and ubiquitin-like (Ub/Ubl) molecules is a potent way to alter protein functions and/or sort specific protein targets to the proteasome for degradation. Many poxviruses interfere with the host Ub/Ubl system by encoding viral proteins that can usurp this pathway. Some of these include viral proteins of the membrane-associated RING-CH (MARCH) domain, p28/Really Interesting New Gene (RING) finger, ankyrin-repeat/F-box and Broad-complex, Tramtrack and Bric-a-Brac (BTB)/Kelch subgroups of the E3 Ub ligase superfamily. Here we describe and discuss the various strategies used by poxviruses to target and subvert the host cell Ub/Ubl systems.

Abbreviations: RING, Really Interesting New Gene, Ub, ubiquitin, Ubl, ubiquitin-like, SUMO, small ubiquitin-like modifiers, ISG15, interferon stimulated gene 15, DUB, deubiquitinating enzyme, USP, Ubl-specific proteases, SCF, Skp1-Cul1-F-box, PRANC, Pox proteins Repeats of ANkyrin-C terminal, BTB, Broad-complex, Tramtrack and Bric-a-Brac, APC/C, anaphase-promoting complex/cyclosome, IAP, inhibitors of apoptosis, BIR, Baculoviral IAP repeat, MARCH, membrane-associated RING-CH

Keywords: Ubiquitin, Poxvirus, RING, MARCH, PRANC/F-box, BTB-BACK-Kelch