Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Mais filtros

Base de dados
Ano de publicação
Tipo de documento
Assunto da revista
País de afiliação
Intervalo de ano de publicação
1.
Immunity ; 36(1): 79-91, 2012 Jan 27.
Artigo em Inglês | MEDLINE | ID: mdl-22209676

RESUMO

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.


Assuntos
Especificidade de Anticorpos , Epitopos de Linfócito T/metabolismo , Complexo Principal de Histocompatibilidade , Receptores de Antígenos de Linfócitos T alfa-beta/metabolismo , Sequência de Aminoácidos , Animais , Deleção de Genes , Ligantes , Camundongos , Dados de Sequência Molecular , Ligação Proteica , Receptores de Antígenos de Linfócitos T alfa-beta/genética , Receptores Virais/metabolismo , Linfócitos T/imunologia , Timo/citologia , Timo/imunologia
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA