流感病毒的vRNP复合体与宿主蛋白的相互作用可以决定流感病毒的传染力和毒力。前期我们已证明宿主MOV10蛋白通过抑制病毒vRNP复合体的入核转运，进而抑制流感病毒的复制过程（已发表）。然而，vRNP复合体的出核转运的机制尚不完全清楚。在本项目中，我们初步发现①宿主RBM14蛋白能够与vRNP复合体的NP亚基结合；②RBM14蛋白能够辅助流感病毒的复制；③RBM14表达降低能够抑制vRNP复合体的出核转运。因此，我们首次提出了RBM14蛋白促进了流感病毒vRNP复合体的出核转运过程，进而辅助流感病毒复制的科学假说。本项目拟明确：①RBM14蛋白与宿主CRM1核转运系统的互作关系；②RBM14蛋白与NP蛋白互作的结构域；③RBM14蛋白所在的核旁斑小体与流感病毒复制的关系。本项目旨在深层解析RBM14蛋白促进vRNP复合体的出核转运的分子机制，这将为抗流感药物的研发提供新的设计策略和科学依据。

The viral RNA polymerase (vRNP) complex is an important determinant of virus pathogenicity and host adaptation. Previously, we demonstrated that host protein MOV10 inhibited the nuclear import of the vRNP, thereby restricted the replication of influenza A virus (doi:10.1128/JVI.03137-15). However, the mechanism by which the nuclear export of vRNP is regulated is poorly characterized. In our preliminary study, we found that RBM14 was co-purified with NP, one of the vRNP components, using TAP-MS assay. Further investigation indicated that RBM14 participates in the replication of influenza A viruses. We also found that the depletion of RBM14 resulted in a significant inhibitory effect on nuclear export of vRNP. Thus, we proposed that RBM14 participates in the nuclear export of vRNP complex and subsequently facilitates the replication of influneza A viruses. Our project will focus on the interaction between RBM14 and CRM1 transport system, the binding domain of RBM14 to NP, and the relationship between paraspeckle bodies and the replication of influenza virus, aiming at finding the particular mechanism that RBM14 participates in the nuclear export of vRNP complex, which may provide a new strategy for anti-influenza viral drug design.