Mapping CD55 function - The structure of two pathogen-binding domains at 1.7 angstrom

P Williams, Y Chaudhry, IG Goodfellow, J Billington, R Powell, OB Spiller, DJ Evans, S Lea*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

52 Citations (Scopus)

Abstract

Decay-accelerating factor (CD55), a regulator of the alternative and classical pathways of complement activation, is expressed on all serum-exposed cells. It is used by pathogens, including many enteroviruses and uropathogenic Escherichia coli, as a receptor prior to infection. We describe the x-ray structure of a pathogen-binding fragment of human CD55 at 1.7 Angstrom resolution containing two of the three domains required for regulation of human complement. We have used mutagenesis to map biological functions onto the molecule; decay-accelerating activity maps to a single face of the molecule, whereas bacterial and viral pathogens recognize a variety of different sites on CD55.

Original languageEnglish
Pages (from-to)10691-10696
Number of pages6
JournalJournal of Biological Chemistry
Volume278
Issue number12
DOIs
Publication statusPublished - 21 Mar 2003

Keywords

  • DECAY-ACCELERATING FACTOR
  • CONTROL PROTEIN MODULE
  • FACTOR DAF
  • CELLULAR RECEPTOR
  • HUMAN-COMPLEMENT
  • RECOMBINANT
  • CELLS
  • ECHOVIRUS-11
  • REPLACEMENT
  • INFECTION

Fingerprint

Dive into the research topics of 'Mapping CD55 function - The structure of two pathogen-binding domains at 1.7 angstrom'. Together they form a unique fingerprint.

Cite this