The Association of Receptor of Activated Protein Kinase C 1(RACK1) with Infectious Bursal Disease Virus Viral Protein VP5 and Voltage-dependent Anion Channel 2 (VDAC2) Inhibits Apoptosis and Enhances Viral Replication
The Association of Receptor of Activated Protein Kinase C 1(RACK1) with Infectious Bursal Disease Virus Viral Protein VP5 and Voltage-dependent Anion Channel 2 (VDAC2) Inhibits Apoptosis and Enhances Viral Replication
复制标题
活化蛋白激酶C 1 (RACK1)受体与传染性法氏囊病病毒蛋白VP5和VDAC2的联合抑制细胞凋亡并增强病毒复制
DOI：
10.1074/jbc.m114.585687
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发表时间：
2015-03-27
影响因子：
4.8
通讯作者：
Zheng, Shijun J.
中科院分区：
文献类型：
--
作者：
Lin, Wencheng;Zhang, Zhiqiang;Zheng, Shijun J.
传染性法氏囊病（IBD）是由IBD病毒（IBDV）引起的一种急性、高度传染性、免疫抑制的禽类疾病。我们之前的报告表明，IBDV VP5通过与电压依赖性阴离子通道2 （VDAC2）的相互作用诱导细胞凋亡。然而，其潜在的分子机制尚不清楚。我们在这里报道了活化蛋白激酶c1受体（RACK1）与VDAC2和VP5相互作用，它们可以形成复合物。我们发现，RACK1过表达抑制IBDV诱导的DF-1细胞凋亡，通过小干扰RNA敲低RACK1诱导凋亡，并激活caspase 9和3，抑制IBDV生长。这些结果表明，在IBDV感染过程中，RACK1通过与VDAC2和VP5的相互作用发挥抗凋亡作用，表明VP5在诱导凋亡过程中对RACK1和VDAC2进行了隔离。
Infectious bursal disease (IBD) is an acute, highly contagious, and immunosuppressive avian disease caused by IBD virus (IBDV). Our previous report indicates that IBDV VP5 induces apoptosis via interaction with voltage-dependent anion channel 2 (VDAC2). However, the underlying molecular mechanism is still unclear. We report here that receptor of activated protein kinase C 1 (RACK1) interacts with both VDAC2 and VP5 and that they could form a complex. We found that overexpression of RACK1 inhibited IBDV-induced apoptosis in DF-1 cells and that knockdown of RACK1 by small interfering RNA induced apoptosis associated with activation of caspases 9 and 3 and suppressed IBDV growth. These results indicate that RACK1 plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5, suggesting that VP5 sequesters RACK1 and VDAC2 in the apoptosis-inducing process.