肠道病毒 71 感染可裂解病毒内部核糖体进入位点驱动翻译的负调控因子。
Enterovirus 71 infection cleaves a negative regulator for viral internal ribosomal entry site-driven translation.
机构信息
Research Center for Emerging Viral Infections, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
出版信息
J Virol. 2013 Apr;87(7):3828-38. doi: 10.1128/JVI.02278-12. Epub 2013 Jan 23.
Abstract
Far-upstream element-binding protein 2 (FBP2) is an internal ribosomal entry site (IRES) trans-acting factor (ITAF) that negatively regulates enterovirus 71 (EV71) translation. This study shows that EV71 infection cleaved FBP2. Live EV71 and the EV71 replicon (but not UV-inactivated virus particles) induced FBP2 cleavage, suggesting that viral replication results in FBP2 cleavage. The results also showed that virus-induced proteasome, autophagy, and caspase activity co-contribute to EV71-induced FBP2 cleavage. Using FLAG-fused FBP2, we mapped the potential cleavage fragments of FBP2 in infected cells. We also found that FBP2 altered its function when its carboxyl terminus was cleaved. This study presents a mechanism for virus-induced cellular events to cleave a negative regulator for viral IRES-driven translation.
摘要
远上游元件结合蛋白 2（FBP2）是一种内部核糖体进入位点（IRES）反式作用因子（ITAF），可负调控肠道病毒 71（EV71）翻译。本研究表明，EV71 感染可裂解 FBP2。活 EV71 和 EV71 复制子（而非 UV 失活的病毒颗粒）诱导 FBP2 裂解，提示病毒复制导致 FBP2 裂解。结果还表明，病毒诱导的蛋白酶体、自噬和半胱天冬酶活性共同促成 EV71 诱导的 FBP2 裂解。利用 FLAG 融合的 FBP2，我们在感染细胞中定位了 FBP2 的潜在裂解片段。我们还发现 FBP2 的羧基末端被切割后改变了其功能。本研究提出了一种机制，即病毒诱导的细胞事件可切割病毒 IRES 驱动翻译的负调控因子。
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