Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55.
J Biol Chem
; 273(46): 30443-7, 1998 Nov 13.
Article
en En
| MEDLINE
| ID: mdl-9804811
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 (KD approximately 3.0 microM) as a result of a very fast dissociation rate constant (kon approximately 10(5) M-1.s-1, koff approximately 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 approximately 80% of the binding energy.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Receptores Virales
/
Glicoproteínas de Membrana
/
Enterovirus Humano B
/
Antígenos CD55
Límite:
Humans
Idioma:
En
Revista:
J Biol Chem
Año:
1998
Tipo del documento:
Article
País de afiliación:
Reino Unido
Pais de publicación:
Estados Unidos