Structure-function analysis of Ia molecules: in-phase insertion mutagenesis of the amino-terminal domain of the E beta k polypeptide chain.
Biochimie
; 70(7): 927-35, 1988 Jul.
Article
em En
| MEDLINE
| ID: mdl-2850019
To identify which segments of the beta 1 domain of the E beta k polypeptide control T cell recognition of antigen, E beta genes were constructed with in-phase insertion mutations. Five independent mutants, with insertions mapping to positions 24, 50 and 93 of the E beta k polypeptide, were obtained. Cell lines expressing these mutated genes were analysed by microfluorometry using a panel of 20 anti-Ek monoclonal antibodies. None of the tested in-phase insertions has resulted in the loss of antibody binding sites. In striking contrast, mutations at position 93 and at a lesser level 50 were indicative of a crucial role of the corresponding regions in T-cell recognition, because they led to significant or complete loss of antigen-presenting function with all but one of the T hybridomas tested. These data are discussed with regard to a model of the foreign antigen binding site of Ia molecules.
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Base de dados:
MEDLINE
Assunto principal:
Antígenos de Histocompatibilidade Classe II
/
Genes MHC da Classe II
/
Mutação
Limite:
Animals
Idioma:
En
Revista:
Biochimie
Ano de publicação:
1988
Tipo de documento:
Article
País de afiliação:
França