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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.


Journal article


J Virol

Publication Date





7694 - 7704


Animals, Binding Sites, CD55 Antigens, Capsid, Capsid Proteins, Cercopithecus aethiops, Crystallography, X-Ray, Enterovirus B, Human, HT29 Cells, Humans, Mutation, Receptors, Virus, Vero Cells, Viral Proteins, Virion