中文摘要：

蛋白质 phosphorylation 是在调整蛋白质功能起一个必要作用的最普通的 translational 以后修正过程之一。Helicoverpa armigera 单身者 nucleopolyhedrovirus (HearNPV )编码 orf2 的 nucleocapsid 蛋白质 HA2 通过它的 WCA 领域，在 phosphorylation，地位应当在到肌动朊聚合的尊重是批评的参予导致病毒的肌动朊聚合的组织。在现在的学习，二个通常认为的 phosphorylation 地点(232Thr 和 250Ser ) 和 HA2 的 WCA 领域上的高度保存的丝氨酸(245Ser ) 被变异，并且他们的显型被 reintroducing 描绘变异的 HA2 进 HearNPV 染色体。病毒的传染性试金证明在 245Ser 忍受 HA2 变化的仅仅 recombinant HearNPV 能生产传染 virions， 232Thr 和 250Ser 变化对病毒致命。然而，肌动朊聚合试金证明忍受 HA2 变化的所有三个病毒仍然能够在主人原子核开始肌动朊聚合，它显示 HA2 上的通常认为的 phosphorylation 地点可以通过另一条未辩别出的小径贡献 HearNPV 复制。

英文摘要：

Protein phosphorylation is one of the most common post-translational modification processes that play an essential role in regulating protein functionality. The Helicoverpa armigera single nucleopolyhedrovirus （HearNPV） orf2-encoded nucleocapsid protein HA2 participates in orchestration of virus-induced actin polymerization through its WCA domain, in which phosphorylation status are supposed to be critical in respect to actin polymerization. In the present study, two putative phosphorylation sites （^232Thr and ^250Ser） and a highly conserved Serine （^245Ser） on the WCA domain of HA2 were mutated, and their phenotypes were characterized by reintroducing the mutated HA2 into the HearNPV genome. Viral infectivity assays demonstrated that only the recombinant HearNPV bearing HA2 mutation at ^245Ser can produce infectious virions, both ^232Thr and ^250Ser mutations were lethal to the virus. However, actin polymerization assay demonstrated that all the three viruses bearing HA2 mutations were still capable of initiating actin polymerization in the host nucleus, which indicated the putative phosphorylation sites on HA2 may contribute to HearNPV replication through another unidentified pathway.