Hou Qiang, Su Jun, Wang Jigui, Li Zhili, Mao Yaping, Wang Shuang, Xi Ji, Liu Weiquan
State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing 100193, PR China.
Virus Res. 2016 Jun 2;217:76-84. doi: 10.1016/j.virusres.2016.03.004. Epub 2016 Mar 10.
Recent reports have indicated that phosphorylation of capsid proteins plays an important role in virion assemblage. Autonomous parvoviruses are among the smallest known viruses with an ssDNA genome enclosed within an icosahedral capsid. Here, we demonstrate that a structural protein (VP2) of one member, mink enteritis virus (MEV), is phosphorylated at serine-221 (Ser221) in vivo. Mutant viruses containing an S221A non-phosphorylatable alanine substitution, or an S221E glutamic acid substitution to mimic serine phosphorylation, were able to express VP2 but had either limited ability or were unable to propagate in feline F81 cells. We propose a new mechanism whereby VP2 phosphorylation plays an essential role in amplification during MEV infection.
最近的报告表明，衣壳蛋白的磷酸化在病毒粒子组装中起重要作用。自主细小病毒是已知最小的病毒之一，其单链DNA基因组包裹在二十面体衣壳内。在这里，我们证明了一种细小病毒——水貂肠炎病毒（MEV）的一种结构蛋白（VP2）在体内的丝氨酸221（Ser221）处被磷酸化。含有S221A不可磷酸化丙氨酸替代物或S221E谷氨酸替代物以模拟丝氨酸磷酸化的突变病毒能够表达VP2，但在猫F81细胞中的增殖能力有限或无法增殖。我们提出了一种新机制，即VP2磷酸化在MEV感染期间的扩增中起关键作用。
