SARS冠状病毒非结构蛋白质NSP3突变体构建及其对类泛素分子DUB活性

发布时间：2018-07-03 18:30

本文选题：SARS冠状病毒 + 非结构蛋白质(NSP)　；参考：《中国生物化学与分子生物学报》2013年11期

【摘要】：SARS冠状病毒(SARS-CoV)非结构蛋白NSP3编码的木瓜蛋白酶样蛋白酶(PLpro)对泛素样分子(Ubl)具有去泛素化酶(DUB)活性,但目前有关NSP3 DUB活性研究的报道甚少.本研究构建包含Nsp3基因N末端不同结构域的突变体,并检测NSP3及其一系列突变体对类泛素分子ISG15和SUMO所修饰蛋白质分子的作用特性.实验结果表明,NSP3及其突变体NSP3AD,NSP3AE,NSP3AF具有一定的去ISG15活性,而其突变体NSP3AC则没有去ISG15(DeISGylation)活性.研究结果提示,SARS NSP3具有一定的体内去ISG15活性,并且这种活性主要依赖于Nsp3基因编码的PLpro.但SARS NSP3及其突变体NSP3AC,NSP3AD,NSP3AE和NSP3AF并不具有去SUMO(DeSUMOylation)活性.SARS冠状病毒NSP3对类泛素样分子作用特性的研究为后续NSP3的生物学特性及其对干扰素通路的调控研究奠定了基础.
[Abstract]:SARS coronavirus (SARS-CoV) nonstructural protein NSP3 encoded papain like protease (PLpro) has deubiquitin (DUB) activity to ubiquitin like molecule (Ubl), but there are few reports about the activity of NSP3DUB in SARS coronavirus (SARS-CoV). In this study, the mutants containing different domains of NSP3 gene N-terminal were constructed, and the effects of NSP3 and its series of mutants on the protein molecules modified by ubiquitin molecules ISG15 and sumo were investigated. The results showed that NSP3 and its mutant NSP3AEN NSP3AF had deISG15 activity, but NSP3AC did not deactivate ISG15 (DeISGylation). The results suggest that SARS NSP3 has a certain activity of deISG15 in vivo, and this activity is mainly dependent on the PLprol encoded by the NSP3 gene. But SARS NSP3 and its mutants NSP3ACN NSP3ADNSP3AE and NSP3AF do not have the activity of SUMO (DeSUMOylation). The study of the interaction of SARS-CoV NSP3 on ubiquitin like molecules lays a foundation for the further study of biological characteristics of NSP3 and its regulation of interferon pathway.
【作者单位】：安徽医科大学研究生院;军事医学科学院放射与辐射医学研究所;
【基金】：国家自然科学基金项目(No.81172799,No.81273231)资助~~
【分类号】：R373

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