Lam W Y, Tang Julian W, Yeung Apple C M, Chiu Lawrence C M, Sung Joseph J Y, Chan Paul K S
Department of Microbiology, 1/F Clinical Science Building, Prince of Wales Hospital, Shatin, New Territories, Hong Kong Special Administrative Region, People's Republic of China.
J Virol. 2008 Mar;82(6):2741-51. doi: 10.1128/JVI.01712-07. Epub 2008 Jan 16.
Avian H5N1 influenza virus causes a remarkably severe disease in humans, with an overall case fatality rate of greater than 50%. Human influenza A viruses induce apoptosis in infected cells, which can lead to organ dysfunction. To verify the role of H5N1-encoded NS1 in inducing apoptosis, the NS1 gene was cloned and expressed in human airway epithelial cells (NCI-H292 cells). The apoptotic events posttransfection were examined by a terminal deoxynucleotidyltransferase-mediated dUTP-biotin nick-end-labeling assay, flow cytometric measurement of propidium iodide, annexin V staining, and Western blot analyses with antibodies specific for proapoptotic and antiapoptotic proteins. We demonstrated that the expression of H5N1 NS1 protein in NCI-H292 cells was sufficient to induce apoptotic cell death. Western blot analyses also showed that there was prominent cleavage of poly(ADP-ribose) polymerase and activation of caspase-3, caspase-7, and caspase-8 during the NS1-induced apoptosis. The results of caspase inhibitor assays further confirmed the involvement of caspase-dependent pathways in the NS1-induced apoptosis. Interestingly, the ability of H5N1 NS1 protein to induce apoptosis was much enhanced in cells pretreated with Fas ligand (the time posttransfection required to reach >30% apoptosis was reduced from 24 to 6 h). Furthermore, 24 h posttransfection, an increase in Fas ligand mRNA expression of about 5.6-fold was detected in cells transfected with H5N1 NS1. In conclusion, we demonstrated that the NS1 protein encoded by avian influenza A virus H5N1 induced apoptosis in human lung epithelial cells, mainly via the caspase-dependent pathway, which encourages further investigation into the potential for the NS1 protein to be a novel therapeutic target.
甲型H5N1禽流感病毒可在人类中引发极为严重的疾病,总体病死率超过50%。甲型人流感病毒可诱导受感染细胞发生凋亡,进而导致器官功能障碍。为验证H5N1编码的NS1在诱导凋亡中的作用,将NS1基因克隆并在人气道上皮细胞(NCI-H292细胞)中表达。转染后通过末端脱氧核苷酸转移酶介导的dUTP生物素缺口末端标记试验、碘化丙啶流式细胞术检测、膜联蛋白V染色以及使用促凋亡和抗凋亡蛋白特异性抗体进行的蛋白质印迹分析来检查凋亡事件。我们证明,H5N1 NS1蛋白在NCI-H292细胞中的表达足以诱导凋亡性细胞死亡。蛋白质印迹分析还显示,在NS1诱导的凋亡过程中,聚(ADP-核糖)聚合酶有明显裂解,且半胱天冬酶-3、半胱天冬酶-7和半胱天冬酶-8被激活。半胱天冬酶抑制剂试验结果进一步证实了半胱天冬酶依赖性途径参与了NS1诱导的凋亡。有趣的是,在用Fas配体预处理的细胞中,H5N1 NS1蛋白诱导凋亡的能力大大增强(达到>30%凋亡所需的转染后时间从24小时缩短至6小时)。此外,转染后24小时,在用H5N1 NS1转染的细胞中检测到Fas配体mRNA表达增加约5.6倍。总之,我们证明甲型禽流感病毒H5N1编码的NS1蛋白主要通过半胱天冬酶依赖性途径在人肺上皮细胞中诱导凋亡,这鼓励进一步研究NS1蛋白作为新型治疗靶点的潜力。