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首页> 美国卫生研究院文献>Frontiers in Molecular Biosciences >Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations
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Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations

机译：粗粒计算机模拟在磷脂双层中组装流感血凝素融合肽

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摘要

Membrane fusion is critical to eukaryotic cellular function and crucial to the entry of enveloped viruses such as influenza and human immunodeficiency virus. Influenza viral entry in the host cell is mediated by a 20–23 amino acid long sequence, called the fusion peptide (FP). Recently, possible structures for the fusion peptide (ranging from an inverted V shaped α-helical structure to an α-helical hairpin, or to a complete α-helix) and their implication in the membrane fusion initiation have been proposed. Despite the large number of studies devoted to the structure of the FP, the mechanism of action of this peptide remains unclear with several mechanisms having been suggested, including the induction of local disorder, promoting membrane curvature, and/or altering local membrane composition. In recent years, several research groups have employed atomistic and/or coarse-grained molecular dynamics (MD) simulations to investigate the matter. In all previous works, the behavior of a single FP monomer was studied, while in this manuscript, we use a simplified model of a tripeptide (TP) monomer of FP (TFP) instead of a single FP monomer because each Influenza Hemagglutinin contains three FP molecules in the biological system. In this manuscript we report findings targeted at understanding the fusogenic properties and the collective behavior of these trimers of FP peptides on a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine model membrane. Here we show how the TFP monomers self-assemble into differently sized oligomers in the presence of the membrane. We measure the perturbation to the structure of the phospholipid membrane caused by the presence of these TFP oligomers. Our work (i) shows how self-assembly of TFP in the presence of the membrane induces non negligible deformation to the membrane and (ii) could be a useful starting point to stimulate discussion and further work targeted to fusion pore formation.
机译：膜融合对于真核细胞功能至关重要，对于包膜病毒（如流感病毒和人类免疫缺陷病毒）的进入也至关重要。流感病毒进入宿主细胞的过程是由20-23个氨基酸长的序列（称为融合肽（FP））介导的。近来，已经提出了融合肽的可能结构（从倒V形α-螺旋结构到α-螺旋发夹，或完整的α-螺旋）及其在膜融合起始中的意义。尽管对FP的结构进行了大量的研究，但是该肽的作用机理仍不清楚，已经提出了几种机理，包括诱导局部紊乱，促进膜曲率和/或改变局部膜组成。近年来，几个研究小组采用了原子和/或粗粒度分子动力学（MD）模拟来研究此问题。在所有先前的工作中，都研究了单个FP单体的行为，而在本文中，我们使用了FP（TFP）的三肽（TP）单体而不是单个FP单体的简化模型，因为每个流感血凝素均包含三个FP生物系统中的分子。在此手稿中，我们报告了旨在了解FP肽三聚体在1-棕榈酰基-2-油酰基-sn-甘油-3-磷酸胆碱模型膜上的融合特性和集体行为的发现。在这里，我们显示了TFP单体在膜的存在下如何自组装成不同大小的低聚物。我们测量由这些TFP低聚物的存在引起的对磷脂膜结构的扰动。我们的工作（i）显示了在膜存在下TFP的自组装如何引起膜的不可忽略的变形，并且（ii）可能是激发讨论和针对融合孔形成的进一步工作的有用起点。

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