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

被引:43
作者
Stuart, AD
McKee, TA
Williams, PA
Harley, C
Shen, S
Stuart, DI
Brown, TDK
Lea, SM
机构
[1] Univ Oxford, Dept Biochem, Mol Biophys Lab, Oxford OX1 3QU, England
[2] Univ Cambridge, Dept Pathol, Div Virol, Cambridge CB2 1QP, England
[3] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England
基金
英国惠康基金;
关键词
D O I
10.1128/JVI.76.15.7694-7704.2002
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:7694 / 7704
页数:11
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