Mumps Virus Nucleoprotein Enhances Phosphorylation of the Phosphoprotein by Polo-Like Kinase 1.
Mumps Virus Nucleoprotein Enhances Phosphorylation of the Phosphoprotein by Polo-Like Kinase 1.
复制标题
腮腺炎病毒核蛋白通过 Polo 样激酶 1 增强磷蛋白的磷酸化。
DOI：
10.1128/jvi.02160-15
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发表时间：
2016
影响因子：
5.4
通讯作者：
He,Biao
中科院分区：
文献类型：
--
作者：
Pickar,Adrian;Zengel,James;Xu,Pei;Li,Zhuo;He,Biao
非节段负义病毒（NNSV）的依赖于RNA的RNA聚合酶（vRdRps）由酶促大蛋白（L）和磷蛋白（P）组成。P是高度磷酸化的，并且其磷酸化在病毒RNA合成中起关键作用。由于NNSV不编码激酶，P被宿主激酶磷酸化。在这项研究中，我们调查的作用，病毒蛋白质在腮腺炎病毒（MuV）P的磷酸化。我们发现，核蛋白（NP）增强P的磷酸化。我们已经确定了丝氨酸/苏氨酸激酶Polo样激酶1（PLK 1）作为宿主激酶，磷酸化P，并发现磷酸化P的PLK 1增强NP。MuVP的PLK 1结合位点定位于S（pS/T）P基序的146 - 148位残基，磷酸化位点定位于S292和S294位残基。因此，假设P的磷酸化可以调节NP形成NP-RNA复合物的能力，从而调节病毒RNA合成。我们的工作表明MuV NP影响P的磷酸化，这表明NP可以通过调节P的磷酸化来调节病毒RNA的合成。
The viral RNA-dependent RNA polymerases (vRdRps) of nonsegmented, negative-sense viruses (NNSVs) consist of the enzymatic large protein (L) and the phosphoprotein (P). P is heavily phosphorylated, and its phosphorylation plays a critical role in viral RNA synthesis. Since NNSVs do not encode kinases, P is phosphorylated by host kinases. In this study, we investigate the roles that viral proteins play in the phosphorylation of mumps virus (MuV) P. We found that nucleoprotein (NP) enhances the phosphorylation of P. We have identified the serine/threonine kinase Polo-like kinase 1 (PLK1) as a host kinase that phosphorylates P and have found that phosphorylation of P by PLK1 is enhanced by NP. The PLK1 binding site in MuV P was mapped to residues 146 to 148 within the S(pS/T)P motif, and the phosphorylation site was identified as residues S292 and S294.IMPORTANCEIt has previously been shown that P acts as a chaperone for NP, which encapsidates viral genomic RNA to form the NP-RNA complex, the functional template for viral RNA synthesis. Thus, it is assumed that phosphorylation of P may regulate NP's ability to form the NP-RNA complex, thereby regulating viral RNA synthesis. Our work demonstrates that MuV NP affects phosphorylation of P, suggesting that NP can regulate viral RNA synthesis by regulating phosphorylation of P.