Virus Genes

, Volume 41, Issue 3, pp 309–318

Interaction of orthopoxviruses with the cellular ubiquitin-ligase system


DOI: 10.1007/s11262-010-0519-y

Cite this article as:
Shchelkunov, S.N. Virus Genes (2010) 41: 309. doi:10.1007/s11262-010-0519-y


Protein modification by ubiquitin or ubiquitin-like polypeptides is important for the fate and functions of the majority of proteins in the eukaryotic cell and can be involved in regulation of various biological processes, including protein metabolism (degradation), protein transport to several cellular compartments, rearrangement of cytoskeleton, and transcription of cytoprotective genes. The accumulated experimental data suggest that the ankyrin-F-box-like and BTB-kelch-like proteins of orthopoxviruses, represented by the largest viral multigene families, interact with the cellular Cullin-1- and Cullin-3-containing ubiquitin-protein ligases, respectively. In addition, orthopoxviruses code for their own RING-domain-containing ubiquitin ligase. In this review, this author discusses the differences between variola (smallpox), monkeypox, cowpox, vaccinia, and ectromelia (mousepox) viruses in the organization of ankyrin-F-box and BTB-kelch protein families and their likely functions.


OrthopoxvirusSmallpox virusHost range genesAnkyrin-F-boxBTB-kelchUbiquitin-protein ligase

Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  1. 1.Institute of Cytology and GeneticsSiberian Branch of the Russian Academy of SciencesNovosibirskRussia