Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1

被引：40

作者：

Asa, Risa ^{[1
]}

Ohno, Takashi ^{[1
]}

Kato, Akihisa ^{[1
]}

Kawaguchi, Yasushi ^{[1
]}

机构：

[1] Univ Tokyo, Inst Med Sci, Int Res Ctr Infect Dis, Dept Infect Dis,Div Viral Infect, Tokyo 1088639, Japan

来源：

MICROBES AND INFECTION | 2007年 / 9卷 / 12-13期

基金：

日本学术振兴会;

关键词：

simplex virus; UL13 protein kinase; phosphorylation;

D O I：

10.1016/j.micinf.2007.07.008

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Herpes simplex virus 1 (HSV-1) UL 13 is a viral protein kinase that regulates optimal viral replication in cell cultures. Identification of substrates of protein kinases is a crucial step to elucidate the mechanism by which they function. Using our developed system to analyze the specific protein kinase activity of UL 13. we have shown that UL1 3 protein kinase directly phosphorylates the viral proteins ICP22 and UL49 previously reported to be putative substrates. We also identified UL41 as a previously unreported and novel substrate of UL13. These data will serve as a basis to clarify the mechanism by which UL13 influences viral replication. (c) 2007 Elsevier Masson SAS. All rights reserved.

引用

页码：1434 / 1438

页数：5

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