Immunoglobulin-like nature of the alpha-chain of a human T-cell antigen/MHC receptor.
Immunoglobulin-like nature of the alpha-chain of a human T-cell antigen/MHC receptor.
复制标题
人类 T 细胞抗原/MHC 受体 α 链的免疫球蛋白样性质。
作者:
Hannum,CH;Kappler,JW;Trowbridge,IS;Marrack,P;Freed,JH
Although the receptor with which T cells bind specific antigen can, like immunoglobulin, distinguish between antigens which differ only slightly in structure, it is unique in recognizing antigen only in conjunction with one of the self proteins of the major histocompatibility complex (MHC restriction)1–4. The receptor was identified and characterized in mouse and man by using monoclonal antibodies to receptor idiotypes5–7, and consists of two disulphide-linked polypeptides, an acidicα-chain and a neutral to slightly basicβ-chain5,8,9. Peptide maps have shown that, like immunoglobulin, both chains vary for receptors of different specificities10–12. T-cell-derived cDNA clones have recently been identified in mouse and man encoding immunoglobulin-like molecules13–15. These were identified as derived fromβ-chain genes through a partial N-terminal protein sequence of theβ-chain isolated from a human T-cell tumour16. We have now purified theα- andβ-chains of the receptor of the human T-cell leukaemia line HPB-MLT, and have determined the amino acid sequence of several tryptic peptides derived from each chain. Our results further confirm that the previously reported cDNA clones encodeβ-chains. The sequence of theα-chain peptides identify this as another immunoglobulin-like polypeptide chain. Particularly striking was anα-chain peptide with high homology to the conserved portion of the immunoglobulin J segment and T-cell receptorβ-chains. Surprisingly, theα-chain peptides show little similarity to the sequence predicted by two overlapping putative murineα-chain cDNA clones17.