PXD016065-1

PXD016065 is an original dataset announced via ProteomeXchange.

Title	Characterization and relative quantitation of wheat, rye and barley gluten protein types by LC-MS/MS
Description	The 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.
HostingRepository	PanoramaPublic
AnnounceDate	2019-10-29
AnnouncementXML	Submission_2019-10-29_12:19:18.xml
DigitalObjectIdentifier
ReviewLevel	Non peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Barbara Lexhaller
SpeciesList	scientific name: Hordeum vulgare; NCBI TaxID: 4513; scientific name: Triticum aestivum; NCBI TaxID: 4565; scientific name: Secale cereale; NCBI TaxID: 4550;
ModificationList	Gln->pyro-Glu; Carbamidomethyl; Oxidation
Instrument	TripleTOF 6600; QTRAP 6500

Revision	Datetime	Status	ChangeLog Entry
0	2019-10-29 05:48:05	ID requested
⏵ 1	2019-10-29 12:19:19	announced
2	2019-12-16 16:53:40	announced	: Added publication

Dataset with its publication pending

submitter keyword: allergy, amylase/trypsin-inhibitor (ATI), celiac disease, gliadin, gluten, mass spectrometry, non-celiac gluten sensitivity (NCGS), proteomics

Katharina Scherf
contact affiliation	Department of Bioactive and Functional Food Chemistry, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Adenauerring 20a, 76131 Karlsruhe, Germany
contact email	k.scherf.leibniz-lsb@tum.de
lab head
Barbara Lexhaller
contact affiliation	Leibniz-Institute for Food Systems Biology at the Technical University of Munich, Lise-Meitner-Str. 34, 85354 Freising, Germany
contact email	b.lexhaller.leibniz-lsb@tum.de
dataset submitter

Panorama Public dataset URI