组氨酸质子化触发病毒膜融合及其分子机制  

Virus member fusion triggered by histidine protonation and its molecular mechanism

作　　者：秦照玲[1,2] 鞠鹤鹏[3] 戚中田[1,2] 

机构地区：[1]第二军医大学微生物学教研室 [2]上海市医学生物防护重点实验室,上海200433 [3]广州军区疾病预防控制中心,广州510000

出　　处：《生命的化学》2014年第5期654-659,共6页Chemistry of Life

基　　金：国家自然科学基金项目(30900066;81171564);上海市重点学科建设项目(B901)

摘　　要：膜融合是有包膜病毒入侵靶细胞的关键步骤,低pH、受体结合、二者兼具或其他尚未界定的机制均可触发病毒融合蛋白的构象重排,介导病毒包膜与靶细胞膜或内体膜间的融合。组氨酸(histidine,His)残基是唯一一个质子化状态变化(pKa^6~7)接近于病毒融合阈值(~pH6)的氨基酸,参与多种低pH依赖的病毒融合蛋白构象转变及膜融合,对其可能作用机制的阐述将有助于抗病毒药物的研制与发展。Member fusion is a critical step of enveloped viruses to enter target cells. The fusion of viral en- velope with target cell membrane or endosomal membrane is mediated by viral fusion protein, whose confor- mational rearrangements can be triggered by low pH, receptor binding, both or other undefined mechanisms. Histidine （His） residue is believed to be involved in low pH- dependent conformational transitions of viral fusion proteins and subsequent member fusion since it is the only residue whose protonation state changes （pKa-6-7） is close to the fusion threshold of viruses at -pH6. The illustration of the possible mechanisms will contribute to the design and development of anti-viral drugs.

关 键 词：有包膜病毒 膜融合 组氨酸 质子化 低PH 

分 类 号：R373[医药卫生—病原生物学]