Relation of antigenic structure of cereal proteins to their toxicity in coeliac patients

• Published in: British journal of nutrition Vol. 53; no. 1; pp. 39 - 45
• Main Authors: Ciclitira, P. J., Ellis, H. J., Evans, D. J., Lennox, E. S.
• Format: Journal Article
• Language: English
• Published: Cambridge, UK Cambridge University Press 1985
• Subjects: analytical methods; Animals; antigens; Biological and medical sciences; celiac disease; Celiac Disease - etiology; Cross Reactions; Epitopes; Gastroenterology. Liver. Pancreas. Abdomen; gliadin; Gliadin - immunology; Gliadin - toxicity; grain crops; Humans; Immune Sera - immunology; inhibitors; Iodine Radioisotopes; Medical sciences; Other diseases. Semiology; Papers of direct relevance to Clinical and Human Nutrition; Plant Proteins - immunology; proteins; Rabbits; Stomach. Duodenum. Small intestine. Colon. Rectum. Anus; Structure-Activity Relationship; toxicity; Antigen; Human; Proteins; Celiac disease; Immunological investigation; Digestive diseases; Cereal; Intestinal disease
• ISSN: 0007-1145; 1475-2662
• DOI: 10.1079/BJN19850008

1. Unfractionated gliadin and its α-, β-, γ- and ω-gliadin subfractions were used as rabbit immunogens. The antisera were characterized by (1) Ouchterlony double diffusion, (2) binding of 125I-labelled gliadin subfractions, (3) inhibition by several gliadin subfractions of binding between γgliadin antiserum and 125I-labeIled γgliadin. 2. Double diffusion showed identical cross-reactivity between the antisera and the gliadin subfractions with the exception of ω-gliadin. Precipitin lines of partial identity with gliadin were observed against rye secalins and barley hordeins but not oat avenins or maize zeins. 3. Binding was observed between unfractionated 125I-labelledα-, β-, γ- and ω-gliadins and all the antisera. There was binding of 125I-labelled ω-gliadin to the ω-gliadin antiserum but poor binding of 125I-labelled ω-gliadin to unfractionated α-, β- and γ-gliadin antisera. Competitive inhibition of binding between 125I-labelled γ-gliadin and γ-gliadin antiserum diluted 1:250 (v/v) demonstrated similar competition between α-, β- and γ-gliadins and this antiserum but poor competition between ω-gliadin, wheat glutenins, albumins and globulins, rye secalins, barley hordeins and oat avenins. 4. These findings suggest that there is a good correlation between the antigenic structure of gliadin proteins and their toxicity to patients with coeliac disease.