Unknown

Dataset Information

0

Immunogenicity characterization of two ancient wheat ?-gliadin peptides related to coeliac disease.

ABSTRACT: The immunogenic potential of ?-gliadin protein from two ancient wheats was studied with reference to coeliac disease. To this aim we investigated Graziella Ra® and Kamut® (the latter is considered an ancient relative of modern durum wheat) in comparison to four durum wheat accessions (Senatore Cappelli, Flaminio, Grazia and Svevo). ELISA and Western Blot analyses - carried out by two monoclonal antibodies raised against the ?-gliadin peptides p31-49 (LGQQQPFPQQPYPQPQPF) and p56-75 (LQLQPFPQPQLPYPQPQLPY) containing a core region (underlined) reported to be toxic for coeliac patients - always showed an antibody-antigen positive reaction. For all accessions, an ?-gliadin gene has also been cloned and sequenced. Deduced amino acid sequences constantly showed the toxic motifs. In conclusion, we strongly recommend that coeliac patients should avoid consuming Graziella Ra® or Kamut®. In fact their ?-gliadin not only is as toxic as one of the other wheat accessions, but also occurs in greater amount, which is in line with the higher level of proteins in ancient wheats when compared to modern varieties.

SUBMITTER: Gregorini A 

PROVIDER: S-EPMC3257593 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Immunogenicity characterization of two ancient wheat α-gliadin peptides related to coeliac disease.

Gregorini Armando A   Colomba Mariastella M   Ellis H Julia HJ   Ciclitira Paul J PJ  

Nutrients 20090201 2

The immunogenic potential of α-gliadin protein from two ancient wheats was studied with reference to coeliac disease. To this aim we investigated Graziella Ra® and Kamut® (the latter is considered an ancient relative of modern durum wheat) in comparison to four durum wheat accessions (Senatore Cappelli, Flaminio, Grazia and Svevo). ELISA and Western Blot analyses - carried out by two monoclonal antibodies raised against the α-gliadin peptides p31-49 (LGQQQPFPQQPYPQPQPF) and p56-75 (LQLQPFPQPQLPY  ...[more]

Similar Datasets

Unknown Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin.
| S-EPMC1131722 | biostudies-other
Unknown Antagonists and non-toxic variants of the dominant wheat gliadin T cell epitope in coeliac disease.
| S-EPMC1856168 | biostudies-literature
Unknown Coeliac disease in infants: antibodies to deamidated gliadin peptide come first!
| S-EPMC5553580 | biostudies-other
Unknown Outlook for coeliac disease patients: towards bread wheat with hypoimmunogenic gluten by gene editing of α- and γ-gliadin gene families.
| S-EPMC6670228 | biostudies-other
Unknown IgA antibodies of coeliac disease patients recognise a dominant T cell epitope of A-gliadin.
| S-EPMC1774203 | biostudies-literature
Unknown Structural Perspective of Gliadin Peptides Active in Celiac Disease.
| S-EPMC7731278 | biostudies-literature
Unknown The production and crystallization of the human leukocyte antigen class II molecules HLA-DQ2 and HLA-DQ8 complexed with deamidated gliadin peptides implicated in coeliac disease.
| S-EPMC2344093 | biostudies-literature
Unknown Persistence of elevated deamidated gliadin peptide antibodies on a gluten-free diet indicates nonresponsive coeliac disease.
| S-EPMC3962785 | biostudies-literature
Unknown Comparative Analysis of in vitro Digestibility and Immunogenicity of Gliadin Proteins From Durum and Einkorn Wheat.
| S-EPMC7326042 | biostudies-literature
Unknown Effective shutdown in the expression of celiac disease-related wheat gliadin T-cell epitopes by RNA interference.
| S-EPMC2947919 | biostudies-literature