doi:10.1016/j.biotechadv.2005.05.005
Copyright © 2005 Elsevier Inc. All rights reserved.
Research review paper
Coeliac Disease: Background and biochemical aspects
References and further reading may be available for this article. To view references and further reading you must
purchase this article.
Rob. J. Hamer
Centre for Protein Technology, WUR Wageningen, The Netherlands
TNO Quality of Life, Zeist, The Netherlands
Received 1 March 2005;
accepted 13 May 2005.
Available online 11 July 2005.
Abstract
Coeliac Disease has to be considered a main food related affliction, with life long consequences for the people having the disease. Coeliac Disease patients suffer from adverse effects that can be related to specific gluten peptide sequences that trigger a sequence of immune related reactions leading to damage of the intestine and related malabsorption symptoms. Recently, detailed information has come available on peptide sequences that are toxic for Coeliac Disease patients. This information is discussed in relation to prevention of the disease and the development of safe cereals for Coeliac Disease patients.
Keywords: Coeliac Disease; Gluten; Peptides
Fig. 2. Example of a toxic sequence in the gliadin molecule. The schematic shows the typical domain structure of gliadin (I–V), with a small part of domain I (marked by *) containing the toxic sequence.
Fig. 3. Phylogenetic tree of cereals. This representation shows how close plants are related. The smaller the distance, the closer the homology. The circle contains the cereals considered toxic to CD patients: Secale (rye), Triticum (wheat, durum), Avena (oats) and Hordeum (barley). Oryza (rice) and Sorghum are more distant; these plants are considered safe.
Table 1.
Positive matches of algorithms with other cereal proteins, from Vader et al. (2000)

Database searches with the search algorithms.
The search algorithms reveal many matches in the gluten, hordeins, and secalin sequences but very few in the avenin sequences. The predictive algorithm 2 (QXPQXP[YFWIL]) and the less strict variants of that algorithm have no matches in the avenin database. The novel T-cells stimulatory gluten peptide (QQPFPQQPQQPFPQ) is also found in the hordeins and secalin but not in the avenins. X stands for any amino acid.
The table shows the number of matches for the various search algorithms for protein sequences from gluten, hordein (barley), secalin (rye) and avenin (oats). This number should be regarded with some caution since the number of sequences available in the database also determines it.
a Algorithm 2 without the specification of a Q at position 4 predicts the known gliadin α9 epitope.
b A proline at p2 in this algorithm inhibits deamidation of the glutamine.