The Journal of Experimental Medicine
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Journal of Experimental Medicine, Vol 169, 2251-2256, Copyright © 1989 by Rockefeller University Press

ARTICLES

Insulin B chain functions as an effective competitor of antigen presentation via peptide homologies present in the thymus

GG Miller, JF Hoy and JW Thomas
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.

The B chain of mammalian insulins contains appropriately spaced amino acids that predict recognition by T cells. However, all T cell clones from an HLA-DR1, Dw6 diabetic donor recognize epitopes associated with the A chain, and the B chain was found to inhibit these responses. Effective intramolecular competition at the level of the APC, not a direct effect on the T cell, is responsible for the inhibition. Insulin B chain contains two clusters of amino acid homology with the TCR beta chain and B chain peptides lacking these clusters do not compete for antigen presentation. A hole in the repertoire for T cells that recognize this portion of the insulin molecule may arise in the thymus by deletion of T cells that recognize similar peptides.
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