The contrasting IgG-binding interactions of human and herpes simplex virus Fc receptors.
Biochem Soc Trans
; 30(4): 495-500, 2002 Aug.
Article
en En
| MEDLINE
| ID: mdl-12196122
A virally encoded, high-affinity Fc receptor (FcR) is found on herpes simplex virus type 1 (HSV-1) particles and infected cells where its binding of non-immune IgG protects cells from host-mediated lysis. Whilst mutation or aglycosylation of the IgG CH2 domain reduced binding to human FcR, the interaction with HSV-1 FcR was not affected. However, the HSV-1 FcR, unlike human FcR, discriminates between human IgG1 allotypes, being sensitive to changes at positions 214 (CH1) and 356/358 (CH3), away from its proposed binding site at the CH2-CH3 interface. The biological consequences are not known but this is the first evidence of a major functional difference between IgG1 allotypes.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Inmunoglobulina G
/
Receptores Fc
/
Herpesvirus Humano 1
Límite:
Humans
Idioma:
En
Revista:
Biochem Soc Trans
Año:
2002
Tipo del documento:
Article
Pais de publicación:
Reino Unido