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甲型流感病毒M1装配的天然结构
作者:小柯机器人 发布时间:2020/9/12 21:37:34

英国医学研究理事会分子生物学实验室John A. G. Briggs和中国科学院广州生物医学与健康研究所Xiaoli Xiong团队合作取得最新进展。他们揭示甲型流感病毒基质蛋白1(M1)装配的天然结构。2020年9月9日出版的《自然》杂志发表了这项成果。

他们确定了完整病毒颗粒内已组装的M1的完整结构,以及在体外重建的M1低聚物的结构。他们发现,M1的C末端结构域在溶液中是无序的,但可以折叠并反式结合到另一个M1单体的N末端结构域,从而使M1聚合成线性链,覆盖组装病毒体膜的内表面。在M1聚合物中,由M1的三个不同单体贡献的五个组氨酸残基形成一个簇,可在进入靶细胞后用作pH敏感的拆解开关。因此,这些结构揭示了流感病毒组装和分解的机制。

据了解,在每年的流行病中,甲型流感病毒可导致数百万例严重疾病。流感病毒粒子中最丰富的蛋白质是M1,它通过在病毒膜下形成内骨骼来介导病毒的装配。全长M1的结构及其寡聚化以介导病毒体装配的方式尚不清楚。

附:英文原文

Title: The native structure of the assembled matrix protein 1 of influenza A virus

Author: Julia Peukes, Xiaoli Xiong, Simon Erlendsson, Kun Qu, William Wan, Leslie J. Calder, Oliver Schraidt, Susann Kummer, Stefan M. V. Freund, Hans-Georg Krusslich, John A. G. Briggs

Issue&Volume: 2020-09-09

Abstract: Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane1. The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues—contributed by three different monomers of M1—form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly.

DOI: 10.1038/s41586-020-2696-8

Source: https://www.nature.com/articles/s41586-020-2696-8

期刊信息

Nature:《自然》,创刊于1869年。隶属于施普林格·自然出版集团,最新IF:43.07
官方网址:http://www.nature.com/
投稿链接:http://www.nature.com/authors/submit_manuscript.html