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PXD016065 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCharacterization and relative quantitation of wheat, rye and barley gluten protein types by LC-MS/MS
DescriptionThe consumption of wheat, rye and barley may cause adverse reactions to wheat such as celiac disease (CD), non-celiac gluten/wheat sensitivity (NCGS) or wheat allergy. The storage proteins (gluten) are known as major triggers, but also other functional protein groups such as α-amylase/trypsin-inhibitors or enzymes are possibly harmful for people suffering of adverse reactions to wheat. Gluten is widely used as a collective term for the complex protein mixture of wheat, rye or barley and can be subdivided into the following gluten protein types (GPTs): α-gliadins, γ-gliadins, ω5-gliadins, ω1,2-gliadins, high- (HMW-GS) and low-molecular-weight glutenin subunits (LMW-GS) of wheat, ω-secalins, HMW-secalins, γ-75k-secalins and γ-40k-secalins of rye and C-hordeins, γ-hordeins, B-hordeins and D-hordeins of barley. GPTs isolated from the flours are useful as reference materials for clinical studies, diagnostics or in food analyses and to elucidate disease mechanisms. A combined strategy of protein separation according to solubility followed by preparative reversed-phase high-performance liquid chromatography (RP-HPLC) was employed to purify the GPTs according to hydrophobicity. Due to the heterogeneity of gluten proteins and their partly polymeric nature, it is a challenge to obtain highly purified GPTs with only one protein group. Therefore, it is essential to characterize and identify the proteins and their proportions in each GPT. In this study, the complexity of gluten from wheat, rye, and barley was demonstrated by identification of the individual proteins employing an undirected proteomics strategy involving liquid chromatography-tandem mass spectrometry (LC-MS/MS) of tryptic and chymotryptic hydrolysates of the GPTs. Different protein groups were obtained and the relative composition of the GPTs was revealed. Multiple reaction monitoring (MRM) LC-MS/MS was used for the relative quantitation of the most abundant gluten proteins. These analyses also allowed the identification of known wheat allergens and CD-active peptides. Combined with functional assays, these findings may shed light on the mechanisms of gluten/wheat-related disorders and may be useful to characterize reference materials for analytical or diagnostic assays more precisely.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterBarbara Lexhaller
SpeciesList scientific name: Hordeum vulgare; NCBI TaxID: 4513; scientific name: Triticum aestivum; NCBI TaxID: 4565; scientific name: Secale cereale; NCBI TaxID: 4550;
ModificationListGln->pyro-Glu; Carbamidomethyl; Oxidation
InstrumentTripleTOF 6600; QTRAP 6500
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-10-29 05:48:05ID requested
12019-10-29 12:19:19announced
22019-12-16 16:53:40announced: Added publication
Publication List
Lexhaller B, Colgrave ML, Scherf KA. Characterization and relative quantitation of wheat, rye and barley gluten protein types by LC-MS/MS. Frontiers in Plant Science. 2019;10:1530
Keyword List
submitter keyword: allergy, amylase/trypsin-inhibitor (ATI), celiac disease, gliadin, gluten, mass spectrometry, non-celiac gluten sensitivity (NCGS), proteomics
Contact List
Katharina Scherf
contact affiliationDepartment of Bioactive and Functional Food Chemistry, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Adenauerring 20a, 76131 Karlsruhe, Germany
contact emailk.scherf.leibniz-lsb@tum.de
lab head
Barbara Lexhaller
contact affiliationLeibniz-Institute for Food Systems Biology at the Technical University of Munich, Lise-Meitner-Str. 34, 85354 Freising, Germany
contact emailb.lexhaller.leibniz-lsb@tum.de
dataset submitter
Full Dataset Link List
Panorama Public dataset URI