Mapping the binding domains on decay accelerating factor (DAF) for haemagglutinating enteroviruses: implications for the evolution of a DAF-binding phenotype

RM Powell, T Ward, [No Value] Goodfellow, JW Almond, DJ Evans*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

Decay accelerating factor (DAF) functions as a cell attachment receptor for a wide range of human enteroviruses, the interaction accounting for the haemagglutination phenotype exhibited by many members of this family. Haemagglutination inhibition assays using purified truncated soluble DAF (sDAF) receptors and short consensus repeat (SCR) domain-specific antibodies have been used to determine the domain(s) of DAF to which the viruses bind. Further sDAF-mediated virus neutralization and biosensor analysis have been used to confirm the virus-binding domains of DAF. Of the four distinct clusters of human enteroviruses, three contain representatives that bind DAF. The majority of DAF-binding enteroviruses occupy the 'CBV-like' cluster, and require SCR domains 2-4 for DAF binding. In contrast, the DAF-binding representatives of the 'ENV70-like' and 'PV-like' clusters require SCR1 for DAF interaction. These studies confirm that DAF binding is a widespread characteristic amongst phylogenetically divergent dusters within the enteroviruses and suggest that the ability to bind DAF may have evolved more than once within this group of viruses.

Original languageEnglish
Pages (from-to)3145-3152
Number of pages8
JournalJournal of General Virology
Volume80
Publication statusPublished - Dec 1999

Keywords

  • INTERCELLULAR-ADHESION MOLECULE-1
  • CELL-SURFACE RECEPTORS
  • FACTOR CD55
  • RHABDOMYOSARCOMA CELLS
  • NUCLEOTIDE-SEQUENCE
  • VIRUS BINDING
  • ECHOVIRUS-7
  • B3
  • COXSACKIEVIRUSES
  • PICORNAVIRUSES

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