Nuclear localization signal regulates porcine circovirus type 2 capsid protein nuclear export through phosphorylation

文献类型： 外文期刊

第一作者： Hou, Qiang

作者： Hou, Qiang;Hou, Shaohua;Jia, Hong;Xin, Ting;Jiang, Yitong;Guo, Xiaoyu;Zhu, Hongfei;Chen, Qing

作者机构：

关键词： Porcine circovirus type 2;Capsid;Nuclear localization signal;Nuclear export;Phosphorylation

期刊名称：VIRUS RESEARCH （ 影响因子：3.303； 五年影响因子：3.445 ）

ISSN： 0168-1702

年卷期： 2018 年 246 卷

页码：

收录情况： SCI

摘要： The open reading frame 2 (ORF2) of Porcine circovirus type 2 (PCV2) encodes the major Capsid (Cap) protein, which self-assembles into virus-like particle (VLP) of similar morphology to the PCV2 virion and accumulates in the nucleus through the N-terminal arginine-rich nuclear localization signal (NIS). In this study, PCV2 Cap protein and its derivates were expressed via the baculovirus expression system, and the cellular localization of the recombinant proteins were investigated using anti-Cap mAb by imaging flow cytometry. Analysis of sub cellular localization of Cap protein and its variants demonstrated that NIS mediated Cap protein nuclear export as well as nuclear import, and a phosphorylation site (S17) was identified by liquid chromatography-tandem mass spectrometry (LC MS/MS) in the NLS domain to regulate Cap protein nuclear export. Phosphorylation of NIS regulating the PCV2 Cap protein nuclear export was also demonstrated in PK15 cells by fluorescence microscopy. Moreover, the influence of Rep and Rep' protein on Cap protein subcellular localization was investigated in PK15 cells. Phosphorylation of NLS regulating Cap protein nuclear export provides more detailed knowledge of the PCV2 viral life cycle.

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