Comparative investigations of gluten proteins from different wheat species. III. N-terminal amino acid sequences of α-gliadins potentially toxic for coeliac patients

  title={Comparative investigations of gluten proteins from different wheat species. III. N-terminal amino acid sequences of $\alpha$-gliadins potentially toxic for coeliac patients},
  author={Herbert Wieser},
  journal={European Food Research and Technology},
  • H. Wieser
  • Published 2001
  • Biology
  • European Food Research and Technology
Abstract. Studies on the coeliac toxicity of wheat have been focused on common (bread) wheat. Other cultivated wheat species were tested in an inadequate manner or were tested not at all. Because in vivo testing by feeding to coeliac patients is out of the question for ethical reasons, the different species were compared by N-terminal sequences of α-gliadins including the potential toxic sequences. Flours of durum wheat, emmer, and einkorn were successively extracted with a salt solution and 60… Expand
Molecular Characterization and Variation of the Celiac Disease Epitope Domains among α-Gliadin Genes in Aegilops tauschii.
Analysis of the neighbor-joining tree demonstrates that 2 of the totally 7 α-gliadins cluster within the homologues of Triticum (A genome), and the other 5 group with those of Aegilops Sitopsis (B genome), which implies that the 7 α -gliadin genes may be originated from the ancestor species of Ae. Expand
Biochemical and molecular characterization of gliadins
The gliadin genes, even prolamin genes, have a common origin and subsequent divergence leads to gene polymorphism, and the rare potential intermolecular disulfide bonds and the long repetitive domains play an important role in the quality of wheat flour. Expand
Molecular characterization of the celiac disease epitope domains in α-gliadin genes in Aegilops tauschii and hexaploid wheats (Triticum aestivum L.)
The five α-gliadin genes were successfully expressed in E. coli, and their expression amount reached to the maximum after 4 h induced by IPTG, indicating that the α- gliadin gene can express in a high level under the control of T7 promoter. Expand
Characterization of α-gliadin genes from diploid wheats and the comparative analysis with those from polyploid wheats
Comparative analysis indicated that the functional α-gliadin genes from A genome are highly conserved, whereas the identity of pseudogenes in diploids wheats are higher than those in hexaploid wheats. Expand
The α-gliadin genes from Brachypodium distachyon L. provide evidence for a significant gap in the current genome assembly
A number of gliadin genes in B. distachyon were isolated, which is contradictory to the results of genome sequencing projects, and Aegilops, Triticum, and Brachypodium species were found to be more closely related. Expand
Gluten—The Precipitating Factor
Cereal seeds are called kernels or grains, and among them wheat, rye, and barley, belonging to the tribe of the Poaceae, are toxic in celiac disease, but oat activity is very low and toxicity has been confirmed only for a small number. Expand
The use of transglutaminase in the reduction of immunoreactivity of wheat flour
Abstract The immune response of wheat flour modified by the treatment with transglutaminase under different conditions of temperature, incubation periods and the ratio of enzyme/wheat flour wasExpand
fluence of proteolysis by subtilisin on the immune reaction of different fractions of wheat proteins, separated from wheat flour. The immunoreactivity of each protein fraction was examined by an indirect non-competitive enzyme-linked immunosorbent assay (ELISA)
Allergy is a continuously increasing medical problem of recent years. As it was estimated, up to 10% of the population depending on the age is affected by food allergies [Estaban, 1992]. Food allergyExpand
A Grounded Guide to Gluten: How Modern Genotypes and Processing Impact Wheat Sensitivity.
A summary of the main pathologies related to wheat in the human body, including celiac disease, wheat allergy, nonceliac wheat sensitivity, fructose malabsorption, and irritable bowel syndrome is provided. Expand
Isolation and Analysis of α-Gliadin Gene Coding Sequences from Triticum durum
Three coding sequences of gliadins genes were isolated from the genomic DNA of Triticum durum accessions CItr5083 and amino acid sequences deduced were characterized with the typical structure of α-gliadin proteins, including the toxic sequences (PSQQQP). Expand


Comparative investigations of gluten proteins from different wheat species II. Characterization of ω-gliadins
Flours of different wheat species were successively extracted with a salt solution and 60% aqueous ethanol and revealed significantly higher proportions of glutamine, proline, and phenylalanine compared with other gluten proteins. Expand
Comparative investigations of gluten proteins from different wheat species I. Qualitative and quantitative composition of gluten protein types
Common wheats were characterised by the highest proportions of total glutenins and HMW subunits, which are known to be important for breadmaking quality, and the lower ratio of gliadins to glutenins was typical. Expand
[Spelt wheat and celiac disease].
  • F. Forssell, H. Wieser
  • Chemistry, Medicine
  • Zeitschrift fur Lebensmittel-Untersuchung und -Forschung
  • 1995
It can be concluded that spelt wheat is a coeliac-toxic cereal and has to be avoided byCoeliac patients. Expand
Deduced Amino Acid Sequence of an α-Gliadin Gene from Spelt Wheat (Spelta) Includes Sequences Active in Celiac Disease
It is concluded that spelta is not a safe grain for people with celiac disease, contrary to the implications in labeling a bread made from spelta as “an alternative to wheat”. Expand
Quantitative Determination of Gluten Protein Types in Wheat Flour by Reversed‐Phase High‐Performance Liquid Chromatography
ABSTRACT A combined extraction-HPLC procedure was developed on a microscale to determine the amounts of the different gluten protein types (ω5-, ω1,2-, α- and γ-gliadins; high molecular weight [HMW]Expand
Effects of Gliadin-Derived Peptides from Bread and Durum Wheats on Small Intestine Cultures from Rat Fetus and Coeliac Children
It is suggested that durum wheat gliadins peptides are in vitro less toxic than bread wheat Gliadin peptides for the small intestinal mucosa of coeliacs as they have less direct cytotoxic effect on the enterocyte. Expand
1 The precipitating factor in coeliac disease
In-vivo testing of gliadin peptides demonstrated that the N-terminal region (domain I) of α-type gliadins is involved in activating coeliac disease, and various in-vitro tests and two in- vivo studies on synthetic peptides support the importance of one or both of these sequences. Expand
Gluten‐sensitive enteropathy (celiac disease)
Most evidence suggests that the mucosal lesion of GSE represents an imraunologicaly mediated tissue injury triggered by gluten ingestion within the context of a particular assortment of major histocompatibility complex genes. Expand
Coeliac activity of the gliadin peptides CT-1 and CT-2
The examination in the organ-culture test including 18 coeliac patients on normal diet and 7 control persons have shown that the toxicity is preserved after the chymotryptic treatment and that the peptides B 3142, CT-1 and CT-2 do not significantly differ from one another according to their coeliakie-specific effect. Expand