Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2)
Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2)
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DOI：
10.1016/j.virusres.2003.10.010
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发表时间：
2004-02-01
期刊：
影响因子：
5
通讯作者：
Baudin, F
中科院分区：
文献类型：
--
作者：
Arzt, S;Petit, I;Baudin, F
流感病毒M1（基质）蛋白在病毒的膜组分和其复制组分八个核糖核蛋白颗粒（RNP）之间形成连接。对于这种活性，M1在受感染的细胞中自我聚合，以将含有糖蛋白的膜片段拉在一起。在感染过程的后期，M1进入细胞核，并在新产生的RNP的核输出过程中活跃，用于病毒颗粒组装。M1的N-末端结构域（残基1-164）携带核定位序列（NLS）基序，对RNP的膜结合、自聚合和核输出很重要。NLS突变体M1已被用于功能研究，以暗示在这三个活动的NLS中的正电荷。在本文中，该NLS突变体的N-末端结构域的晶体结构被确定，并被发现是相同的野生型蛋白质，清楚地表明，这是不存在的带正电荷的残基的NLS，导致敲除表型，而不是在突变蛋白的整体结构的变化。(C)2003 Elsevier B. V.保留所有权利。
The influenza virus M1 (matrix) protein forms the connection between the membrane component of the virus and its replication component eight ribonucleoprotein particles (RNPs). For this activity, M1 self-polymerises in the infected cell in order to pull glycoprotein containing membrane segments together. Later in the process of infection, M1 enters the nucleus and is active in the nuclear export process of newly made RNPs for virus particle assembly. The N-terminal domain (residues 1-164) of M1 carries the nuclear localisation sequence (NLS) motif and is important for membrane binding, self-polymerisation and nuclear export of RNPs. An NLS-mutant M1 has been used in functional studies in order to implicate the positive charges in the NLS in these three activities. In this paper, the crystal structure of the N-terminal domain of this NLS-mutant is determined and is found to be the same as that of the wild-type protein, clearly indicating that it is the absence of the positively charged residues of the NLS that causes the knock-out phenotype rather than a change in the overall structure of the mutant protein. (C) 2003 Elsevier B.V. All rights reserved.