A monoclonal antibody that recognizes a potential coeliac-toxic repetitive pentapeptide epitope in gliadins.
Osman, Awad A. a; Uhlig, Holm H. b; Valdes, Israel c; Amin, Mona a; Mendez, Enrique c; Mothes, Thomas a
[Article] European Journal of Gastroenterology & Hepatology. 13(10):1189-1193, October 2001.

(Format: HTML, PDF)

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.