宿主细胞中的泛素特异性蛋白酶9X与单纯疱疹病毒1型ICP0相互作用。
Ubiquitin-specific protease 9X in host cells interacts with herpes simplex virus 1 ICP0.
作者信息
Sato Yuka, Kato Akihisa, Arii Jun, Koyanagi Naoto, Kozuka-Hata Hiroko, Oyama Masaaki, Kawaguchi Yasushi
机构信息
Division of Molecular Virology, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108-8639, Japan.
出版信息
J Vet Med Sci. 2016 Mar;78(3):405-10. doi: 10.1292/jvms.15-0598. Epub 2015 Nov 21.
Herpes simplex virus 1 (HSV-1) expresses infected cell protein 0 (ICP0), a multi-functional protein with E3 ubiquitin ligase activity and a critical regulator of the viral life cycle. To obtain novel insights into the molecular mechanism by which ICP0 regulates HSV-1 replication, we analyzed HEp-2 cells infected with HSV-1 by tandem affinity purification and mass spectrometry-based proteomics. This screen identified 50 host-cell proteins that potentially interact with ICP0, including ubiquitin-specific protease 9X (USP9X). The interaction between ICP0 and USP9X was confirmed by co-immunoprecipitation. Notably, USP9X depletion increased the ICP0 abundance and promoted viral replication. These results suggest that USP9X-dependent regulation of ICP0 expression is part of a complex feedback mechanism that facilitates optimal HSV-1 replication.
单纯疱疹病毒1型（HSV-1）表达感染细胞蛋白0（ICP0），这是一种具有E3泛素连接酶活性的多功能蛋白，也是病毒生命周期的关键调节因子。为了深入了解ICP0调节HSV-1复制的分子机制，我们通过串联亲和纯化和基于质谱的蛋白质组学分析了感染HSV-1的HEp-2细胞。该筛选鉴定出50种可能与ICP0相互作用的宿主细胞蛋白，包括泛素特异性蛋白酶9X（USP9X）。通过共免疫沉淀证实了ICP0与USP9X之间的相互作用。值得注意的是，USP9X的缺失增加了ICP0的丰度并促进了病毒复制。这些结果表明，USP9X对ICP0表达的依赖性调节是促进HSV-1最佳复制的复杂反馈机制的一部分。
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