Abstract
The wheat varietal selection undertaken by breeders in recent decades has been tailored mainly to improve technological and productivity-related traits; however, the latter has resulted in a considerable impoverishment of the genetic diversity of wheat-based products available on the market. This pitfall has encouraged researchers to revalue the natural diversity of cultivated and non-cultivated wheat genotypes in light of their different toxic/immunogenic potential for celiac disease and wheat-allergic patients. In the present investigation, an advanced proteomic approach was designed for the global characterization of the protein profile of selected tetraploid wheat genotypes (Triticum turgidum). The approach combined proteins/peptides sequence information retrieved by specific enzymatic digestions (single and dual proteolytic enzymes) with protein digestibility information disclosed by means of in-vitro simulated human gastroduodenal digestion experiments. In both cases, the peptide pools were characterized by discovery analysis with liquid chromatography high-resolution tandem mass spectrometry, and specific amino acid sequences were identified via commercial software. The peptide list was screened for in silico toxicity/immunogenicity risk assessment, with the aid of various open-source bioinformatics tools for epitopes matching. Given the global information provided by the designed proteomic approach, the in silico risk assessment not only tackled toxicity implication for celiac disease patients, but also scouted for immunogenic sequences relevant for wheat allergic patients, achieving a comprehensive characterization of the protein profile of the selected genotypes. These latter were assessed to encrypt a variable number of toxic/immunogenic epitopes for celiac disease and wheat allergy, and as such they could represent convenient bases for breeding practices and for the development of new detoxification strategies.
Highlights
Wheat is one of the most important and widely consumed cereals in the world, and it is the preferred choice for bread and pasta making, due to its peculiar technological properties
Gliadins are divided into subgroups α, β, γ, and ω according to their electrophoretic mobility in acid PAGE, while glutenin subunits are classified as either high molecular weight (HMW-GS, type-x, or type-y) or low molecular weight (LMW-GS, s, m- and i-type) [4]
Looking at the distribution of the sequences encrypting wheat allergies (WA) epitopes among different proteins, we found that the albumin/globulin immunogenic sequences were not detectable in GD digests, either as intact sequences or as hydrolyzed fragments; we can conclude that they were completely hydrolyzed by digestive enzymes at the end of the duodenal phase
Summary
Wheat is one of the most important and widely consumed cereals in the world, and it is the preferred choice for bread and pasta making, due to its peculiar technological properties. The albumin/globulin proteins account for about the 20% of the total grain proteins. They include water and salt-soluble proteins and are mainly represented by metabolic, regulatory and protective enzymes involved in important functions related to the development of the plant and responses to the environment [2,3]. The storage proteins are represented by gluten proteins, which are classified as monomeric, alcohol-soluble prolamins (gliadins) and polymeric, alcohol-insoluble glutelins (glutenins). Gliadins are divided into subgroups α, β, γ, and ω according to their electrophoretic mobility in acid PAGE, while glutenin subunits are classified as either high molecular weight (HMW-GS, type-x, or type-y) or low molecular weight (LMW-GS, s-, m- and i-type) [4]
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