Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission.
Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission.
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DOI：
10.1038/srep44695
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发表时间：
2017-03-20
影响因子：
4.6
通讯作者：
Rossman JS
中科院分区：
文献类型：
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作者：
Martyna A;Bahsoun B;Badham MD;Srinivasan S;Howard MJ;Rossman JS
从内吞作用到病毒出芽，细胞膜断裂是所有出芽过程中的关键步骤。许多蛋白质与断裂有关，尽管断裂是如何完成的基本分子细节通常仍然未知。在这里，我们调查的过程中M2介导的膜断裂的流感病毒的萌芽。病毒M2蛋白的残基50-61结合膜并形成两亲性α-螺旋（AH）。膜结合需要与脂质尾部的疏水相互作用，但不需要与脂质头部基团的带电相互作用。在结合时，M2 AH诱导膜弯曲和脂质有序化，使膜颈收缩和不稳定，引起断裂。我们进一步表明，AH在细胞蛋白Arf 1和Epsin 1的行为以类似的方式。它们共同代表一类膜诱导的AH结构域，其改变膜曲率和流动性，在多种生物途径中介导收缩的膜颈的断裂。
Membrane scission is a crucial step in all budding processes, from endocytosis to viral budding. Many proteins have been associated with scission, though the underlying molecular details of how scission is accomplished often remain unknown. Here, we investigate the process of M2-mediated membrane scission during the budding of influenza viruses. Residues 50–61 of the viral M2 protein bind membrane and form an amphipathic α-helix (AH). Membrane binding requires hydrophobic interactions with the lipid tails but not charged interactions with the lipid headgroups. Upon binding, the M2AH induces membrane curvature and lipid ordering, constricting and destabilizing the membrane neck, causing scission. We further show that AHs in the cellular proteins Arf1 and Epsin1 behave in a similar manner. Together, they represent a class of membrane-induced AH domains that alter membrane curvature and fluidity, mediating the scission of constricted membrane necks in multiple biological pathways.