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

G. G. Miller, J. F. Hoy, J. W. Thomas

Research output: Contribution to journalArticleResearchpeer-review

7 Citations (Scopus)


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 β 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.

Original languageEnglish
Pages (from-to)2251-2256
Number of pages6
JournalJournal of Experimental Medicine
Issue number6
Publication statusPublished - 1 Jan 1989

Cite this