A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.

A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein.
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DOI:
10.1016/j.jmb.2004.06.044
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发表时间:
2004-08-13
影响因子:
5.6
通讯作者:
Arkin IT
Arkin IT
中科院分区:
生物学2区
文献类型:
--
作者:
Arbely E;Khattari Z;Brotons G;Akkawi M;Salditt T;Arkin IT

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导致最近严重急性呼吸系统综合征(SARS)爆发的病原体是一种以前未被识别的冠状病毒。虽然有大量的流行病学研究,但很少有SARS冠状病毒(SCoV)蛋白的分子特征。在这里,我们描述了SCoV E蛋白的分子特征,该蛋白是负责病毒体包膜形态发生的病毒的关键组成部分。我们最终表明,SCoV E蛋白包含一个异常短,回文跨膜螺旋发夹周围的一个以前未确定的伪对称中心,这似乎是唯一的SCoV的结构特征。发夹通过增加曲率使脂质双层变形,首次提供了E蛋白在病毒出芽中的关键作用的分子解释。对SCoV这一关键组分的分子理解可能代表了旨在抑制其功能并因此抑制病毒感染性的协同努力的开始。
The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV. The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity.
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