A herpesvirus ubiquitin-specific protease is critical for efficient T cell lymphoma formation
A herpesvirus ubiquitin-specific protease is critical for efficient T cell lymphoma formation
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DOI：
10.1073/pnas.0706295104
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发表时间：
2007-12-11
影响因子：
11.1
通讯作者：
Osterrieder, Nikolaus
中科院分区：
文献类型：
--
作者：
Jarosinski, Keith;Kattenhorn, Lisa;Osterrieder, Nikolaus
疱疹病毒泛素特异性蛋白酶（USP）家族，其创始成员被发现为嵌入单纯疱疹病毒1（HSV-1）的大被膜蛋白中的蛋白酶结构域，在疱疹病毒科的所有成员中是保守的。这种保守性是否表明酶在体内的基本功能尚未确定。如本文所报道的，USP活性在马立克氏病病毒（MDV）（一种致瘤性α-疱疹病毒）中是保守的。消除MDV大皮层蛋白USP活性的单个氨基酸取代减少了MDV在体内的复制，并严重限制了病毒的致癌潜力。USP转录本在MDV转化细胞系中的表达进一步证实了这一假设。因此，疱疹病毒USP似乎不仅需要在免疫活性宿主中保持立足点，而且还有助于恶性生长。
The herpesvirus ubiquitin-specific protease (USP) family, whose founding member was discovered as a protease domain embedded in the large tegument protein of herpes simplex virus 1 (HSV-1), is conserved across all members of the Herpesviridae. Whether this conservation is indicative of an essential function of the enzyme in vivo has not yet been established. As reported here, USP activity is conserved in Marek's disease virus (MDV), a tumorigenic alpha-herpesvirus. A single amino acid substitution that abolishes the USP activity of the MDV large tegument protein diminishes MDV replication in vivo, and severely limits the oncogenic potential of the virus. Expression of the USP transcripts in MDV-transformed cell lines further substantiates this hypothesis. The herpesvirus USP thus appears to be required not only to maintain a foothold in the immunocompetent host, but also to contribute to malignant out-growths.