INSERM U758, Human Virology Department, Université de Lyon, Claude Bernard University Lyon-1, Ecole Normale Supérieure de Lyon, Lyon, France.
J Infect Dis. 2011 Nov;204 Suppl 3:S934-40. doi: 10.1093/infdis/jir320.
Ebola virus (EBOV) transcription is dependent on the phosphoprotein VP30, a component of the viral nucleocapsid. VP30 is phosphorylated at 2 serine residue clusters located at the N-terminal part of the protein. In this report, we have investigated the role of VP30 phosphorylation in EBOV replication using a reverse genetics approach. In effect, recombinant EBOVs with the VP30 serine clusters substituted either by nonphosphorylatable alanines or phosphorylation-mimicking aspartates were generated and characterized. We show that in comparison to the wild-type EBOV the mutated viruses possess reduced infectivity. This difference is explained by alterations in the balance between the transcription and replication processes and appear to be associated with the state of VP30 phosphorylation. Here we propose a model in which dynamic phosphorylation of VP30 is an important mechanism to regulate the EBOV replication cycle.
埃博拉病毒 (EBOV) 的转录依赖于磷蛋白 VP30，它是病毒核衣壳的一个组成部分。VP30 在位于蛋白质 N 端部分的 2 个丝氨酸残基簇上被磷酸化。在本报告中，我们使用反向遗传学方法研究了 VP30 磷酸化在 EBOV 复制中的作用。实际上，生成并表征了 VP30 丝氨酸簇被非磷酸化丙氨酸或磷酸化天冬氨酸取代的重组 EBOV。我们发现与野生型 EBOV 相比，突变病毒的感染性降低。这种差异是由于转录和复制过程之间平衡的改变引起的，并且似乎与 VP30 磷酸化状态有关。在这里，我们提出了一个模型，其中 VP30 的动态磷酸化是调节 EBOV 复制周期的重要机制。
