Interactions between NKG2x immunoreceptors and HLA-E ligands display overlapping affinities and thermodynamics.
J Immunol
; 174(5): 2878-84, 2005 Mar 01.
Article
en En
| MEDLINE
| ID: mdl-15728498
ABSTRACT
The NKG2x/CD94 family of C-type lectin-like immunoreceptors (x = A, B, C, E, and H) mediates surveillance of MHC class Ia cell surface expression, often dysregulated during infection or tumorigenesis, by recognizing the MHC class Ib protein HLA-E that specifically presents peptides derived from class Ia leader sequences. In this study, we determine the affinities and interaction thermodynamics between three NKG2x/CD94 receptors (NKG2A, NKG2C, and NKG2E) and complexes of HLA-E with four representative peptides. Inhibitory NKG2A/CD94 and activating NKG2E/CD94 receptors bind HLA-E with indistinguishable affinities, but with significantly higher affinities than the activating NKG2C/CD94 receptor. Despite minor sequence differences, the peptide presented by HLA-E significantly influenced the affinities; HLA-E allelic differences had no effect. These results reveal important constraints on the integration of opposing activating and inhibitory signals driving NK cell effector functions.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Termodinámica
/
Células Asesinas Naturales
/
Receptores Inmunológicos
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Antígenos de Histocompatibilidad Clase I
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Antígenos HLA
Idioma:
En
Revista:
J Immunol
Año:
2005
Tipo del documento:
Article
País de afiliación:
Estados Unidos