Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.
Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions.
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DOI：
10.1099/vir.0.82809-0
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发表时间：
2007-08
期刊：
影响因子：
--
通讯作者：
Digard P
中科院分区：
文献类型：
--
作者：
Noton SL;Medcalf E;Fisher D;Mullin AE;Elton D;Digard P
甲型流感病毒的基质(M1)蛋白是一种多功能蛋白，在病毒生命周期中发挥着重要的结构和功能作用。它驱动病毒发芽，是病毒粒子的主要蛋白质成分，在病毒被膜和完整膜蛋白与基因组核糖核蛋白(RNPs)之间形成中间层。它还有助于控制RNPs在细胞内的贩运。这些作用主要是通过蛋白质-蛋白质与病毒和可能的细胞蛋白质相互作用来实现的。在这里，识别了参与结合病毒RNPs和介导同源寡聚的M1区域。在体外，通过使用重组蛋白，发现M1的中间结构域负责与NP结合，这种相互作用不需要RNA。同样，只有含有中间结构域的M1多肽能够与从纯化病毒中分离的RNP-M1复合体结合。当检测M1的自结合时，蛋白质的所有三个结构域都参与了同源齐聚，尽管同样地，中间结构域是主导的，并且在没有N-末端和C-末端结构域的情况下有效地自结合。然而，当M1的单个片段被绿色荧光蛋白标记并在病毒感染的细胞中表达时，对丝状颗粒的显微镜观察显示，只有全长的M1被掺入萌芽中的病毒粒子中。结果表明，M1的中间结构域主要负责结合NP和自结合，但需要额外的相互作用才能有效地将M1整合到病毒颗粒中。
The matrix (M1) protein of influenza A virus is a multifunctional protein that plays essential structural and functional roles in the virus life cycle. It drives virus budding and is the major protein component of the virion, where it forms an intermediate layer between the viral envelope and integral membrane proteins and the genomic ribonucleoproteins (RNPs). It also helps to control the intracellular trafficking of RNPs. These roles are mediated primarily via protein–protein interactions with viral and possibly cellular proteins. Here, the regions of M1 involved in binding the viral RNPs and in mediating homo-oligomerization are identified. In vitro, by using recombinant proteins, it was found that the middle domain of M1 was responsible for binding NP and that this interaction did not require RNA. Similarly, only M1 polypeptides containing the middle domain were able to bind to RNP–M1 complexes isolated from purified virus. When M1 self-association was examined, all three domains of the protein participated in homo-oligomerization although, again, the middle domain was dominant and self-associated efficiently in the absence of the N- and C-terminal domains. However, when the individual fragments of M1 were tagged with green fluorescent protein and expressed in virus-infected cells, microscopy of filamentous particles showed that only full-length M1 was incorporated into budding virions. It is concluded that the middle domain of M1 is primarily responsible for binding NP and self-association, but that additional interactions are required for efficient incorporation of M1 into virus particles.
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