Nerenberg Bianca T Hovey, Taylor John, Bartee Eric, Gouveia Kristine, Barry Michele, Früh Klaus
Vaccine and Gene Therapy Institute, Oregon Health and Science University, Beaverton, Oregon 97006, USA.
J Virol. 2005 Jan;79(1):597-601. doi: 10.1128/JVI.79.1.597-601.2005.
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.
痘病毒的环状结构域蛋白p28是一种毒力因子,其分子功能尚不清楚。许多含环状结构域的细胞蛋白作为泛素连接酶(环状E3),将选定的底物蛋白连接到泛素化机制上。在这里,我们证明痘苗病毒p28及其在黏液瘤病毒中的同源物M143R可以介导多聚泛素缀合物的形成,而p28和M143R的环状结构域突变体则不能。此外,p28在体内被泛素化,并且泛素与p28在病毒工厂中共定位,这与完整的环状结构域无关。这些结果表明泛素系统与痘病毒毒力有关。