Your browser version may not work well with NCBI's Web applications. More information here...
1: J Virol. 2002 Aug;76(15):7694-704.Click here to read Click here to read Links

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.

Stuart AD, McKee TA, Williams PA, Harley C, Shen S, Stuart DI, Brown TD, Lea SM.

Division of Virology, Department of Pathology, University of Cambridge, Cambridge CB2 1QP, United Kingdom.

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.

PMID: 12097583 [PubMed - indexed for MEDLINE]

PMCID: PMC136386

Structures reported by this article

  • Echovirus 11
    PDB: 1H8T
    Source: Human echovirus 11
    Method: X-Ray Diffraction | Resolution: 2.9 Å