Identification of reactive synthetic gliadin peptides specific for coeliac disease

J. M. Deverya, V. Bender, I. Penttila, J. H. Skerritt

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Gluten intolerance (coeliac disease) is characterised by the development of a small intestinal lesion followingexposure to the gliadin fraction after consumption of wheat and related cereals. Cellular immune mechanisms are thought to be responsible for gliadin toxicity, but the toxic sequence/s within gliadin have not been clearly established. A panel of synthetic gliadin peptides was tested using peripheral blood mononuclear cells from coeliac patients and two assays for cell-mediated immunity. Using the indirect leucocyte migration inhibition factor and the macrophage procoagulant activity assays, gliadin peptides which were located in the aminoterminal or the proline-rich domain of the alpha/beta gliadin molecule were coeliac-active. Peptides predicted by T cell algorithms or on the basis of homology to adenovirus Ad12 Elb protein and which were located in the proline-poor gliadin domains were inactive. Protein sequence studies which indicate significant homology in the proline-poor gliadin domains with a number of non-coeliac-toxic seed proteins also supported the hypothesis that the prolinc-rich domains may be more important in the pathogenesis of coeliac disease.

Original languageEnglish
Pages (from-to)356-362
Number of pages7
JournalInternational Archives of Allergy and Immunology
Volume95
Issue number4
DOIs
Publication statusPublished - 1 Jan 1991
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this