The poxviral RING protein p28 is a ubiquitin ligase that targets ubiquitin to viral replication factories.
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.
Nerenberg
Bianca T Hovey
BT
Vaccine and Gene Therapy Institute, Oregon Health and Science University, Beaverton, Oregon 97006, USA.
Taylor
John
J
Bartee
Eric
E
Gouveia
Kristine
K
Barry
Michele
M
Früh
Klaus
K
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
D025801:Ubiquitin; D014764:Viral Proteins; D044767:Ubiquitin-Protein Ligases