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

Leiliang Zhang, Nancy Y. Villa, Grant McFadden

Research output: Contribution to journalShort surveypeer-review

40 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)607-614
Number of pages8
JournalFEBS Letters
Issue number4
StatePublished - Feb 18 2009
Externally publishedYes


  • BTB-BACK-Kelch
  • PRANC/F-box
  • Poxvirus
  • RING
  • Ubiquitin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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