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Interactions of decay-accelerating factor (DAF) with haemagglutinating human enteroviruses: utilizing variation in primate DAF to map virus binding sites

Yasmin Chaudhry^1,

Ian G. Goodfellow^1,

¹ Faculty of Biomedical and Life Sciences, Division of Virology, University of Glasgow, Glasgow G11 5JR, UK
² Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, UK

Correspondence
David J. Evans
David.Evans{at}vir.gla.ac.uk

A cellular receptor for the haemagglutinating enteroviruses (HEV), and the protein that mediates haemagglutination, is the membrane complement regulatory protein decay accelerating factor (DAF; CD55). Although primate DAF is highly conserved, significant differences exist to enable cell lines derived from primates to be utilized for the characterization of the DAF binding phenotype of human enteroviruses. Thus, several distinct DAF-binding phenotypes of a selection of HEVs (viz. coxsackievirus A21 and echoviruses 6, 7, 11–13, 29) were identified from binding and infection assays using a panel of primate cells derived from human, orang-utan, African Green monkey and baboon tissues. These studies complement our recent determination of the crystal structure of SCR₃₄ of human DAF [Williams, P., Chaudhry, Y., Goodfellow, I. G., Billington, J., Powell, R., Spiller, O. B., Evans, D. J. & Lea, S. (2003). J Biol Chem 278, 10691–10696] and have enabled us to better map the regions of DAF with which enteroviruses interact and, in certain cases, predict specific virus–receptor contacts.

Present address: School of Animal and Microbial Sciences, University of Reading, PO Box 228, Reading, UK.

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