αß T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities.
Immunity
; 36(1): 79-91, 2012 Jan 27.
Article
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| MEDLINE
| ID: mdl-22209676
ABSTRACT
Major histocompatibility complex (MHC) restriction is the cardinal feature of T cell antigen recognition and is thought to be intrinsic to αß T cell receptor (TCR) structure because of germline-encoded residues that impose MHC specificity. Here, we analyzed αßTCRs from T cells that had not undergone MHC-specific thymic selection. Instead of recognizing peptide-MHC complexes, the two αßTCRs studied here resembled antibodies in recognizing glycosylation-dependent conformational epitopes on a native self-protein, CD155, and they did so with high affinity independently of MHC molecules. Ligand recognition was via the αßTCR combining site and involved the identical germline-encoded residues that have been thought to uniquely impose MHC specificity, demonstrating that these residues do not only promote MHC binding. This study demonstrates that, without MHC-specific thymic selection, αßTCRs can resemble antibodies in recognizing conformational epitopes on MHC-independent ligands.
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1
Banco de datos:
MEDLINE
Asunto principal:
Receptores de Antígenos de Linfocitos T alfa-beta
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Epítopos de Linfocito T
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Complejo Mayor de Histocompatibilidad
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Especificidad de Anticuerpos
Límite:
Animals
Idioma:
En
Año:
2012
Tipo del documento:
Article