Viral interaction with the host cell sumoylation system.

Abstract

A novel host cell post-translational modification system termed sumoylation was discovered recently. Sumoylation is an enzymatic process that is biochemically analogous to, but functionally distinct from ubiquitinylation. As in ubiquitinylation, sumoylation involves the attachment of a small protein moiety, SUMO, to substrate proteins. Conjugation of SUMO does not typically lead to degradation of the substrate and instead causes functional alterations or changes in intracellular localization. While the majority of identified SUMO targets are cellular proteins, both herpesvirus and papillomavirus proteins have also been identified as authentic substrates for this modification. The exact effect of sumoylation on viral proteins appears to be substrate specific, but does have functional consequences that are likely to be important for the viral life cycle. In addition to viral proteins being targets for sumoylation, there is both direct and indirect evidence that viruses can alter the sumoylation status of host cell proteins. Such modulation of critical host proteins may be important for inhibiting cellular defense mechanisms or for promoting an intracellular state that is supportive of viral reproduction. This review highlights the enzymology of sumoylation and discusses the known examples of how viruses impact and are impacted by sumoylation.