Demonstration of the presence of coeliac-activating gliadin-like epitopes in malted barley

International Archives of Allergy and Immunology
Heather J EllisPaul J Ciclitira

Abstract

A peptide B3144, derived after peptic tryptic digestion of alpha-gliadin and corresponding to residues 3-56 from the coeliac-activating domain I, was previously used to produce monoclonal antibodies. A dot immunobinding assay was developed using these antibodies to detect gluten in wheat, rye, barley and oats. The limit of sensitivity of the assay was 1 microgram/ml for unfractionated wheat gliadin and rye prolamins, and 5 micrograms/ml for barley and oat prolamins. Extracts of flours from coeliac non-toxic rice, maize, millet and sorghum gave negative results. Malt, which represents a partial hydrolysate of barley prolamins, was shown to contain the equivalent of 100-200 mg of barley prolamins/100 g of malt. The assay demonstrates the presence of intact epitopes from the coeliac-activating domain I of alpha-gliadins in malted barley, suggesting toxicity.

Citations

Jun 1, 2005·Best Practice & Research. Clinical Gastroenterology·Paul J CiclitiraKnut E A Lundin
Jan 20, 1999·Alimentary Pharmacology & Therapeutics·N D Parnell, P J Ciclitira
May 16, 1998·The New England Journal of Medicine·N ParnellP Ciclitira
Oct 31, 2006·Food Additives and Contaminants·P DostálekD Gabrovská
Sep 24, 2015·Journal of Food Science and Technology·Mekonnen Melaku GebremariamThomas Becker
Feb 26, 2013·Journal of Agricultural and Food Chemistry·Paola PontieriLuigi Del Giudice

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