Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation
Influenza Virus M2 Ion Channel Protein Is Necessary for Filamentous Virion Formation
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DOI：
10.1128/jvi.00119-10
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发表时间：
2010-05-01
影响因子：
5.4
通讯作者：
Lamb, Robert A.
中科院分区：
文献类型：
--
作者：
Rossman, Jeremy S.;Jing, Xianghong;Lamb, Robert A.
甲型流感病毒从细胞中芽出球形（直径约为100纳米）和丝状（直径约为100纳米× 2至20 μ m）病毒粒子。先前的工作已经确定，基质蛋白（M1）赋予病毒形成细丝的能力；然而，进一步的研究表明，流感病毒M2整体膜蛋白在病毒丝的形成中也起作用。在检查M2蛋白在丝形成中的作用时，我们观察到M2的细胞质尾部包含几个对丝形成至关重要的位点。此外，虽然M2是一种非筏蛋白，但在流感病毒感染的情况下，其他病毒蛋白的表达会导致M2与病毒出芽和脂质筏结构域共定位。我们发现位于M2细胞质尾部的一个两亲螺旋能够结合胆固醇，我们推测M2胆固醇结合对丝的形成和现有病毒丝的稳定性都是必不可少的。
Influenza A virus buds from cells as spherical (similar to 100-nm diameter) and filamentous (similar to 100 nm x 2 to 20 mu m) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a nonraft protein, expression of other viral proteins in the context of influenza virus infection leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We found that an amphipathic helix located within the M2 cytoplasmic tail is able to bind cholesterol, and we speculate that M2 cholesterol binding is essential for both filament formation and the stability of existing viral filaments.