A monoclonal antibody that recognizes a potential coeliac-toxic repetitive pentapeptide epitope in gliadins

Eur J Gastroenterol Hepatol. 2001 Oct;13(10):1189-93. doi: 10.1097/00042737-200110000-00011.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / metabolism*
  • Celiac Disease / genetics*
  • Celiac Disease / immunology
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / genetics*
  • Epitopes / immunology
  • Food Analysis
  • Gliadin / genetics*
  • Gliadin / immunology
  • Glutens / genetics
  • Humans
  • Molecular Sequence Data


  • Antibodies, Monoclonal
  • Epitopes
  • Glutens
  • Gliadin