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首页> 外文期刊>Biopolymers: Original Research on Biomolecules and Biomolecular Assemblies >The Impact of Influenza Hemagglutinin Fusion Peptide Length and Viral Subtype on Its Structure and Dynamics
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The Impact of Influenza Hemagglutinin Fusion Peptide Length and Viral Subtype on Its Structure and Dynamics

机译：流感血凝素融合肽长度和病毒亚型对其结构和动力学的影响

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摘要

A peptide comprising no fewer than the first 20 residues of the influenza hemagglutinin HA2 subunit suffices to induce lipid mixing between the membranes of different unilamellar vesicles. This 20-residue peptide was previously reported to adopt an open "boomerang" structure that differs significantly from the closed helicalhairpin structure of a fusion peptide consisting of the first 23 residues of the HA2 sequence. This study investigates the structural and dynamic features of fusion peptides of different length and subtype. Lacking key interactions that stabilize the closed, helical-hairpin structure, the 20- residue peptide is in a dynamic equilibrium between closed and open states, adopting a ca. 11% population of the former when solubilized by DPC micelles. Peptides shorter than 20 residues would have even fewer interactions to stabilize a helical hairpin fold, resulting in a vanishing hairpin population. Considering the conserved nature of hairpin-stabilizing interactions across all serotypes, and the minimum of 20 residues needed for fusion, we postulate that the closed state plays an essential role in the fusion process. However, opening of this hairpin structure may be essential to the formation of a membrane pore at the final stage of the fusion process.
机译：包含不少于流感血凝素HA2亚基的前20个残基的肽足以诱导不同单层囊泡膜之间的脂质混合。先前报道该20个残基的肽采用开放的“回旋镖”结构，该结构与由HA2序列的前23个残基组成的融合肽的闭合的螺旋发夹结构显着不同。这项研究调查了不同长度和亚型的融合肽的结构和动力学特征。缺少稳定闭合螺旋发夹结构的关键相互作用，因此20个残基的肽在闭合状态和打开状态之间处于动态平衡，采用ca值。当被DPC胶束溶解时，前者的人口为11％。少于20个残基的肽具有更少的相互作用来稳定螺旋状发夹折叠，从而使发夹数量消失。考虑到所有血清型之间发夹稳定相互作用的保守性质，以及融合所需的最少20个残基，我们假设闭合状态在融合过程中起着至关重要的作用。然而，在融合过程的最后阶段，打开这种发夹结构对于形成膜孔可能是必不可少的。

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