Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55

SM Lea*, RM Powell, T McKee, DJ Evans, D Brown, DI Stuart, PA van der Merwe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

66 Citations (Scopus)

Abstract

The biochemical properties of the molecular interactions mediating viral-cell recognition are poorly characterized. In this study, we use surface plasmon resonance to study the affinity and kinetics of the interaction of echovirus 11 with its cellular receptor decay-accelerating factor (CD55). As reported for interactions between cell-cell recognition molecules, the interaction has a low affinity (K-D similar to 3.0 mu m) as a result of a very fast dissociation rate constant (k(on) similar to 10(5) m(-1). s(-1), k(off) -0.3 s(-1)). This contrasts with the interaction of soluble ICAM-1 (sICAM-1, CD54) with human rhinovirus 3 which has been reported to have a similar affinity but 10(2)-10(3)-fold slower kinetics (Casasnovas, J. M., and Springer, T. A (1995) J. Biol. Chem. 270, 13216-13224). The extracellular portion of decay-accelerating factor comprises four short consensus repeat domains (domains 1-4) and a mucin-like stalk. By comparison of the binding affinity for echovirus 11 of various fragments of decay-accelerating factor, we are able to conclude that short consensus repeat domain 3 contributes similar to 80% of the binding energy.

Original languageEnglish
Pages (from-to)30443-30447
Number of pages5
JournalJournal of Biological Chemistry
Volume273
Issue number46
Publication statusPublished - 13 Nov 1998

Keywords

  • DECAY-ACCELERATING FACTOR
  • INTERCELLULAR-ADHESION MOLECULE-1
  • BINDING
  • COMPLEMENT
  • RHINOVIRUS
  • DOMAINS
  • ICAM-1
  • BIOSENSOR
  • PROTEIN
  • CLONING

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