Accession Number | <strong>00042737-200110000-00011</strong>. |
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Author | Osman, Awad A. a; Uhlig, Holm H. b; Valdes, Israel c; Amin, Mona a; Mendez, Enrique c; Mothes, Thomas a |
Institution | Departments 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 |
Title | |
Source | European Journal of Gastroenterology & Hepatology. 13(10):1189-1193, October 2001. |
Abstract | Objectives: 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. |