COELIAC DISEASE - SPECIFIC TOXICOLOGICAL AND IMMUNOLOGICAL STUDIES OF PEPTIDES FROM a-GLIADINS

摘要

Coeliac disease (CD) may be defined as a primary immune response of the upper small intestine to the storage proteins of wheat, rye and barley (= antigen) and to tissue transglutaminase (= autoantigen) in genetically susceptible individuals. The disease is characterised by a flat mucosa and, in consequence, by the generalised malabsorption of nutrients. The CD lesion is mainly induces by production of interferon y (IFN) by gluten specific T cells. Peptides corresponding to amino acid residues 57-68, 62-75 and 57-73 of a-gliadins have been proposed as the immunodominant epitopes in the majority of CD patients1'2. Deamidation of glutamine residue at position 65 (Q65) to glutamic acid (E65) was necessary for optimal T cell activation. We wished to investigate whether such immunoactive epitopes exacerbate CD in vivo and which residues are essential for T cell stimulation.