title: The poxviral RING protein p28 is a ubiquitin ligase that targets ubiquitin to viral replication factories.
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.
authors.affiliation: Vaccine and Gene Therapy Institute, Oregon Health and Science University, Beaverton, Oregon 97006, USA.
authors.forename: Bianca T Hovey
authors.initials: BT
authors.lastname: Nerenberg
authors.forename: John
authors.initials: J
authors.lastname: Taylor
authors.forename: Eric
authors.initials: E
authors.lastname: Bartee
authors.forename: Kristine
authors.initials: K
authors.lastname: Gouveia
authors.forename: Michele
authors.initials: M
authors.lastname: Barry
authors.forename: Klaus
authors.initials: K
authors.lastname: Früh
mesh_terms: D002460:Cell Line; D006367:HeLa Cells; D006801:Humans; D009154:Mutation; D009233:Myxoma virus; D025801:Ubiquitin / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*; D014616:Vaccinia virus / Q000201:enzymology* / Q000472:pathogenicity*; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014774:Virulence; D014779:Virus Replication
chemical_list: D025801:Ubiquitin; D014764:Viral Proteins; D044767:Ubiquitin-Protein Ligases