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.

Journal article

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.

Authors: Stuart, A; McKee, T; Williams, P; Harley, C; Shen, S

• Publication status: Published
• Journal: Journal of virology
• Volume: 76
• Issue: 15
• Pages: 7694-7704
• Publication date: 2002-08-01
• DOI: 10.1128/jvi.76.15.7694-7704.2002
• EISSN: 1098-5514
• ISSN: 0022-538X
• Language: English
• Keywords: Viral Proteins; Capsid Proteins; Binding Sites; Antigens, CD55; Virion; Crystallography, X-Ray; Mutation; Capsid; Humans; HT29 Cells; Receptors, Virus; Cercopithecus aethiops; Vero Cells; Animals; Enterovirus B, Human