The Journal of Experimental Medicine
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Journal of Experimental Medicine, Vol 184, 1017-1026, Copyright © 1996 by Rockefeller University Press


ARTICLES

A single T cell receptor recognizes structurally distinct MHC/peptide complexes with high specificity

MD Tallquist, TJ Yun and LR Pease
Department of Immunology, Mayo Foundation, Rochester, Minnesota 55905, USA.

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.
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