The MS(E)-proteomic analysis of gliadins and glutenins in wheat grain identifies and quantifies proteins associated with celiac disease and baker's asthma

Abstract

Precise content of gliadin (Glia) and glutenin (Glu) proteins in wheat grain are largely unknown despite their association with celiac disease, various allergies, and physical processing properties of wheat. Developing methods to quantitatively measure clinically relevant proteins could support advancement in understanding exposure thresholds and clinical study design. The aim of this study was to use a data-independent mass spectrometry (MS(E)) approach for quantifying gliadin and glutenin proteins in wheat grain. The biologically replicated analysis yielded concentrations for 34 gliadin and 22 glutenin proteins. The primary focus of this survey was on measuring celiac disease proteins and baker's asthma associated proteins along with the proteins associated with viscoelastic properties of wheat flour and grain texture. The technical coefficients of variation ranged from 0.12 to 1.39 and indicate that MS(E) proteomics is a reproducible quantitative method for the determination of gliadin and glutenin content in the highly complex matrix of protein extracts from wheat grain. This article is part of a Special Issue entitled: Translational Plant Proteomics.

Keywords: CV; GFP; Glia; Gliadins; Glu; Glu-1-fibrinopeptide B; Glutenins; HMW GS; LMW GS; MS(E); MSE; Proteomics; Quantification; Wheat grain; coefficient of variations; data-independent mass spectrometry; emPAI; exponentially modified protein abundance index; high molecular weight glutenin subunits; low molecular weight glutenin subunits; protein fraction containing mostly gliadins; protein fraction containing mostly glutenins.