对11型艾柯病毒的一种衰变加速因子结合临床分离株的结构测定，有助于绘制出对感染的受体需求发生改变的突变体图谱。
Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection.
作者信息
Stuart Amanda D, McKee Thomas A, Williams Pamela A, Harley Chris, Shen Shuo, Stuart David I, Brown T David K, Lea Susan M
机构信息
Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom.
出版信息
J Virol. 2002 Aug;76(15):7694-704. doi: 10.1128/jvi.76.15.7694-7704.2002.
Abstract
We have used X-ray crystallography to determine the structure of a decay accelerating factor (DAF)-binding, clinic-derived isolate of echovirus 11 (EV11-207). The structures of the capsid proteins closely resemble those of capsid proteins of other picornaviruses. The structure allows us to interpret a series of amino acid changes produced by passaging EV11-207 in different cell lines as highlighting the locations of multiple receptor-binding sites on the virion surface. We suggest that a DAF-binding site is located at the fivefold axes of the virion, while the binding site for a distinct but as yet unidentified receptor is located within the canyon surrounding the virion fivefold axes.
摘要
我们利用X射线晶体学确定了衰变加速因子（DAF）结合的、临床分离的11型艾柯病毒（EV11-207）的结构。衣壳蛋白的结构与其他小RNA病毒的衣壳蛋白结构极为相似。该结构使我们能够将EV11-207在不同细胞系中传代产生的一系列氨基酸变化解释为突出了病毒体表面多个受体结合位点的位置。我们认为，一个DAF结合位点位于病毒体的五重轴处，而一个不同但尚未确定的受体的结合位点位于围绕病毒体五重轴的峡谷内。
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