论文摘要
2002年底爆发于中国广东的“非典”型肺炎,世界卫生组织命名为严重急性呼吸道综合症（severe acute respiratory syndrome,SARS）,其病原菌为一种新的冠状病毒,即SARS冠状病毒（SARS related coronavirus,SARS-CoV）。SARS冠状病毒为单链正义RNA病毒,其基因组为已知RNA病毒中最大的。SARS冠状病毒主要蛋白酶(又称3CLpro),分子量为33.8KD,由于其水解加工复制酶前体多聚蛋白ppla与pplab,并释放病毒RNA复制所需的聚合酶与解螺旋酶。因此,3CLpro在病毒的生活周期中起着重要作用,为抗SARS病毒的有效药物靶点。 SARS冠状病毒主要蛋白酶3CLpro,其活性形式为两个同源单体形成的二聚体。每一单体由N-端七肽（N-finger:SGFRKMA）,结构域Ⅰ、Ⅱ、Ⅲ（Domain Ⅰ、Ⅱ、Ⅲ）以及连接结构域Ⅱ与结构域Ⅲ的Loop环组成。酶活性中心位于结构域Ⅰ与Ⅱ之间的间隙中。为研究N-finger对酶活性的作用,我们构建了SARS冠状病毒主要蛋白酶3CLpro及其缺失N-端七肽即N-finger的突变体3CLpro(△1-7)表达质粒,并于大肠杆菌表达系统中表达并纯化。研究发现,去除N-finger的突变体3CLpro(△1-7)丧失了野生型所具有的对荧光底物（Dabcyl-KTSAVLQSGFRKM E-Edans）水解活性,表明处于非酶活性中心的N-finger是酶活性所必需的。利用固相多肽合成法,我们进一步合成了N-finger。酶抑制实验表明N-finger表现了对3CLpro部分抑制活性。本实验结果为抗SARS冠状病毒药物设计提供了全新的思路。
论文目录
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