Arp2/3复合体是引起细胞肌动蛋白聚合的主要效应分子。近年来随着细胞核内肌动蛋白聚合现象的发现，Arp2/3复合体的核转运机制与核内功能愈发引起重视。杆状病毒感染会引起昆虫宿主细胞Arp2/3复合体发生核转运并导致核内肌动蛋白聚合，以辅助新生病毒颗粒的装配。该特点使杆状病毒感染体系成为研究Arp2/3复合体核转运机制与核内功能的理想细胞模型。通过构建杆状病毒基因瞬时表达文库并逐一检测病毒基因对Arp2/3复合体亚细胞定位的影响，我们发现病毒晚期基因Ac34可以诱导昆虫细胞Arp2/3-P40亚基发生核转运。本课题将在此基础上继续验证Ac34对Arp2/3复合体其他亚基的作用，并探索Ac34诱导Arp2/3复合体发生核转运的分子机制。我们的研究不仅有助于深入理解杆状病毒诱导肌动蛋白聚合的分子机制，更加在细胞生物学层面为探索核内肌动蛋白聚合以及Arp2/3复合体核转运机制与核内功能打下基础。

Arp2/3 complex is the primary actin polymerization branching factor. With the discovery of the nuclear actin polymerization, more and more attention has been paid to the Arp2/3 complex nuclear translocation mechanism and nuclear function. One of the unique features of baculovirus infecting insect cell is the nuclear actin polymerization and the Arp2/3 complex nuclear translocation, which provides an elegant cell model for the research of Arp2/3 complex nuclear translocation mechanism and function. To reveal which viral genes are responsible for the Arp2/3 complex nuclear translocation, a transient expression library of AcMNPV ORFs was constructed to screen candidate viral genes that mediate the nuclear relocation of Arp2/3 complex. By co-expression of each viral gene product and Arp2/3 complex in insect cells, we found Ac34 can mediate the nuclear relocation of Arp2/3-P40 subunit. We will continue to explore the effect of Ac34 on other Arp2/3 complex subunits and detailed molecular mechanism of Ac34 nuclear relocation of Arp2/3 complex. Our research will not only extend our understanding of baculovirus-induced actin polymerization, but also shed light on the function of the nuclear Arp2/3 complex.