Abstract
This review summarizes the background of celiac disease (CD), and the available bioinformatic and analytical methods designed to evaluate the molecular aspects of celiac-toxic proteins and peptides. CD is a T-cell-mediated autoimmune disease of the small intestine that is induced by ingestion of gluten proteins from wheat, barley, rye, and, rarely, after consumption of oats. This disease is characterized by malabsorption of nutrients from the intestine. It has been demonstrated that polypeptide chains of gliadin contain repeating amino acid sequences that constitute epitopes for a respective lymphocyte receptor (TCR). It was reported that the optimal length of a polypeptide chain suitable for a TCR is 10 to 15 amino acid residues. Celiac toxic proteins and peptides were characterized by the following methods and techniques: immunochemical, electrophoretic, chromatographic, and mass spectrometric. Characterization of celiac toxic peptides may provide sufficient information to breed out these sequences from wheat, barley or rye, whilst retaining its baking properties. An improved understanding of the immune response to gluten has provided an insight into possible future advances in the treatment of celiac disease.
Acknowledgments
This work was supported by grant PBZ-KBN-097/PZ06/2003/1.1.