The poxviral RING protein p28 is a ubiquitin ligase that targets ubiquitin to viral replication factories

Bianca T. Hovey Nerenberg, John Taylor, Eric Bartee, Kristine Gouveia, Michele Barry, Klaus Früh

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

The poxviral RING protein p28 is a virulence factor whose molecular function is unknown. Many cellular RING-containing proteins act as ubiquitin ligases (RING-E3s) connecting selected substrate proteins to the ubiquitination machinery. Here we demonstrate that vaccinia virus p28 and its homologue in myxoma virus, M143R, can mediate the formation of polyubiquitin conjugates, while RING mutants of both p28 and M143R cannot. Furthermore, p28 is ubiquitinated in vivo and ubiquitin colocalizes with p28 to virus factories independently of an intact RING domain. These results implicate the ubiquitin system in poxviral virulence.

Original languageEnglish (US)
Pages (from-to)597-601
Number of pages5
JournalJournal of virology
Volume79
Issue number1
DOIs
StatePublished - Jan 2005

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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