European Journal of Gastroenterology & Hepatology

Accession Number<strong>00042737-200110000-00011</strong>.
AuthorOsman, Awad A. a; Uhlig, Holm H. b; Valdes, Israel c; Amin, Mona a; Mendez, Enrique c; Mothes, Thomas a
InstitutionDepartments of (a)Laboratory Medicine, Clinical Chemistry and Molecular Diagnostics and of (b)Paediatrics, University Hospital, Leipzig, Germany and (c)Structural Analysis of Proteins Unit, Centro Nacional de Biotecnologia, Cantoblanco, Madrid, Spain
TitleA monoclonal antibody that recognizes a potential coeliac-toxic repetitive pentapeptide epitope in gliadins.[Article]
SourceEuropean Journal of Gastroenterology & Hepatology. 13(10):1189-1193, October 2001.
AbstractObjectives: Antibodies that detect coeliac-toxic prolamins from wheat, barley and rye are important tools for controlling the diet of coeliac disease patients. Recently, a monoclonal antibody R5 that recognizes wheat gliadin, barley hordein and rye secalin equally was described. In this study, the epitope recognized by R5 was investigated.

Methods: Both a phage-displayed heptapeptide library and overlapping peptides spanning the sequence of [alpha]- and [gamma]-type gliadins (pepscan) were screened for binding of R5.

Results: Both techniques yielded comparable pentapeptide consensus sequences (phage display QXPW/FP; pepscan QQPFP). According to recent observations, this peptide stretch may be of key importance in the pathogenicity of coeliac disease. This sequence occurs repetitively in prolamins (in [gamma]- and [omega]-type prolamins more frequently than in [alpha]-type prolamins) together with several homologous peptide stretches, which are recognized less strongly.

Conclusions: R5 seems to be a good candidate for the specific detection of putative coeliac disease-active sequences in prolamins and thus represents a valuable tool for the quality control of gluten-free food.

(C) 2001 Lippincott Williams & Wilkins, Inc.