Title Functional Analysis of the Inhibitor of Apoptosis Genes in Antheraea pernyi Nucleopolyhedrovirus
Author Feng Yan1,2, Xiaobei Deng2, Junpeng Yan2, Jiancheng Wang3, Lunguang Yao3, Songya lv2, Yipeng Qi2, and Hua Xu1*
Address 1Department of Urology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Hubei, Wuhan 430030, P. R. China, 2State Key Laboratory of Virology, College of life science, Wuhan University, Wuhan, Hubei 430072, P. R. China, 3Funiushan Henan Key Laboratory of Insect Biology, Nanyang Normal University, Nanyang, Henan 473061, P. R. China
Bibliography Journal of Microbiology, 48(2),199-205, 2010,
Key Words apoptosis, ApNPV, iap, phage display
Abstract The inhibitor of apoptosis proteins (IAP) plays an important role in cell apoptosis. We cloned two novel IAP family members, Ap-iap1 and Ap-iap2, from Antheraea pernyi nucleopolyhedrovirus (ApNPV) genome. Ap-IAP1 contains two baculoviral IAP repeat (BIR) domains followed by a RING domain, but Ap-IAP2 has only one BIR domain and RING. The result of transient expression in Spodoptera frugiperda (Sf21) showed that Ap-iap1 blocked cell apoptosis induced by actinomycin D treatment and also rescued the p35 deficient Autographa californica nucleopolyhedrovirus (AcNPV) to replicate in Sf9 cells, while Ap-iap2 does not have this function. Several Ap-IAP1 truncations were constructed to test the activity of BIRs or RING motif to inhibit cell apoptosis. The results indicated that BIRs or RING of Ap-IAP1 had equally function to inhibit cell apoptosis. Therefore deletion of above both of the above domains could not block apoptosis induced by actinomycin D or rescue the replication of AcMNPV△p35. We also screened two phage-display peptides that might interact with Ap-IAP1.