Inhibition of alloreactive cytotoxic T lymphocytes by peptides from the alpha 2 domain of HLA-A2.
Class I major histocompatibility complex (MHC) molecules function in the recognition of antigens by cytotoxic T lymphocytes (CTL). Although this biological role is firmly established and much has been learnt about their structure and polymorphic variation, little is known of the regions of class I molecules that are involved in functional interactions with components of the T-cell surface. Here we show that peptides derived from residues 98-113 of the alpha 2 domain of HLA-A2 specifically inhibit the recognition of target cells by many HLA-A2-specific CTL. In addition to identifying a region that is probably involved in binding the T-cell receptor these results raise the possibility that alloreactive CTL may recognize degraded fragments of class I histocompatibility antigens.
D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000494:pharmacology; D019286:Endopeptidase K; D010450:Endopeptidases / Q000494:pharmacology; D000939:Epitopes / Q000276:immunology; D006680:HLA Antigens / Q000032:analysis*; D015789:HLA-A2 Antigen; D010455:Peptides / Q000032:analysis*; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology*
D000939:Epitopes; D006680:HLA Antigens; D015789:HLA-A2 Antigen; D010455:Peptides; D010450:Endopeptidases; D002918:Chymotrypsin; D019286:Endopeptidase K