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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 SCR(34) 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.

Original publication

DOI

10.1099/vir.0.19674-0

Type

Journal article

Journal

J Gen Virol

Publication Date

03/2004

Volume

85

Pages

731 - 738

Keywords

Amino Acid Sequence, Animals, Antigens, CD55, Binding Sites, Conserved Sequence, Cricetinae, Enterovirus, Hemagglutination Tests, Humans, Models, Molecular, Molecular Sequence Data, Papio, Phenotype, Primates, Protein Conformation, Sequence Alignment, Sequence Homology, Amino Acid