Tallquist M D, Yun T J, Pease L R
Department of Immunology, Mayo Foundation, Rochester, Minnesota 55905, USA.
J Exp Med. 1996 Sep 1;184(3):1017-26. doi: 10.1084/jem.184.3.1017.
The 2C T cell is a CD8+, alloreactive T cell, which recognizes cells bearing Ld and Kbm3 class I major histocompatability complex molecules. Here, we characterize an allopeptide, designated dEV-8, that is a ligand in the Kbm3 molecule for the 2C TCR but is not a ligand in the Ld molecule. By biochemical and immunological properties, dEV-8 is distinct from P2Ca, the Ld allopeptide that is also recognized by the 2C TCR. Using the deduced amino acid sequence of dEV-8, we isolate a candidate endogenous source of the peptide. The endogenous protein, MLRQ, contains a peptide sequence identical to dEV-8. This degenerate recognition of two distinct peptide/MHC complexes by a single TCR has important implications for understanding allorecognition.
2C T细胞是一种CD8 +的同种异体反应性T细胞,它识别携带Ld和Kbm3 I类主要组织相容性复合体分子的细胞。在此,我们鉴定了一种名为dEV - 8的别位肽,它是Kbm3分子中2C TCR的配体,但不是Ld分子的配体。从生化和免疫学特性来看,dEV - 8与P2Ca不同,P2Ca是Ld别位肽,也能被2C TCR识别。利用dEV - 8推导的氨基酸序列,我们分离出了该肽的候选内源性来源。内源性蛋白质MLRQ包含与dEV - 8相同的肽序列。单个TCR对两种不同肽/MHC复合物的这种简并识别对于理解同种异体识别具有重要意义。