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Keywords = omega-5 gliadin

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21 pages, 633 KB  
Review
Basophil Activation Test in IgE-Mediated Wheat Allergy: Diagnostic and Clinical Applications—A Narrative Review
by Elena Camelia Berghea, Mădălina Coman-Stanemir and Ioana Raluca Papacocea
Diagnostics 2025, 15(20), 2659; https://doi.org/10.3390/diagnostics15202659 - 21 Oct 2025
Viewed by 1647
Abstract
The basophil activation test (BAT) is an emerging tool in the diagnosis and management of IgE-mediated wheat allergies (WAs), particularly in complex or high-risk phenotypes. This narrative review explores the clinical applications of BAT across a spectrum of WA presentations, including wheat-dependent exercise-induced [...] Read more.
The basophil activation test (BAT) is an emerging tool in the diagnosis and management of IgE-mediated wheat allergies (WAs), particularly in complex or high-risk phenotypes. This narrative review explores the clinical applications of BAT across a spectrum of WA presentations, including wheat-dependent exercise-induced anaphylaxis (WDEIA), contact urticaria, and pediatric food allergy. The BAT provides a functional measure of allergen-triggered basophil activation, bridging the gap between mere sensitization and true clinical reactivity. We highlight its utility in detecting sensitization to specific wheat components such as ω-5 gliadin, glutenin subunits, and hydrolyzed wheat proteins, and its value in cases where traditional diagnostics are inconclusive. Furthermore, BAT is discussed as a dynamic biomarker in therapeutic monitoring, especially in patients receiving omalizumab, where reduced basophil reactivity correlates with improved clinical outcomes. While standardization and access remain challenges, the BAT holds significant promise as a precision diagnostic and monitoring tool in wheat allergies. Full article
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16 pages, 5619 KB  
Article
Allelic Analysis of the Gli-B1 Locus in Hexaploid Wheat Using Reverse-Phase–Ultra-Performance Liquid Chromatography
by Jong-Yeol Lee, Yu-Jeong Yang, Jinpyo So, Sewon Kim and Kyoungwon Cho
Molecules 2025, 30(3), 609; https://doi.org/10.3390/molecules30030609 - 30 Jan 2025
Cited by 1 | Viewed by 1434
Abstract
Wheat (Triticum aestivum L.) omega-5 gliadin, a major allergen responsible for wheat-dependent exercise-induced anaphylaxis in humans, is encoded by genes located at the Gli-B1 locus on chromosome 1B, which exhibits genetic polymorphism. Gli-B1 alleles have generally been identified based on the electrophoretic [...] Read more.
Wheat (Triticum aestivum L.) omega-5 gliadin, a major allergen responsible for wheat-dependent exercise-induced anaphylaxis in humans, is encoded by genes located at the Gli-B1 locus on chromosome 1B, which exhibits genetic polymorphism. Gli-B1 alleles have generally been identified based on the electrophoretic mobilities of the encoded gamma-, omega-1,2, and omega-5 gliadins in acid polyacrylamide gel electrophoresis. However, the similar mobilities of omega-5 gliadin variants make it difficult to distinguish them among different wheat varieties. In this study, we optimized reverse-phase–ultra-performance liquid chromatography (RP-UPLC) conditions to separate omega-5 gliadins in the reference wheat cultivar Chinese Spring and its nullisomic–tetrasomic lines for chromosome 1B. Five chromatographic peaks corresponded to omega-5 gliadin, and the average relative standard deviation to each peak retention time ranged from 0.31% to 0.93%, indicating that the method is accurate and reproducible for fractionating omega-5 gliadins in gliadin extracts from wheat flour. Using the optimized RP-UPLC method, we analyzed omega-5 gliadins in 24 wheat varieties with the Gli-B1f allele. The result showed that the wheat varieties were sorted into eight groups according to the composition of omega-5 gliadin, indicating that the classification of Gli-B1 alleles based on A-PAGE could not explain the composition of omega-5 gliadin in wheat. We reclassified 73 wheat varieties containing 16 unique Gli-B1 alleles into 31 groups based on the chromatographic patterns of their omega-5 gliadins. Our results provide information on the specific Gli-B1 alleles of wheat varieties belonging to each group and demonstrate the potential for RP-UPLC to facilitate genetic studies of wheat varieties. Full article
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16 pages, 479 KB  
Review
Allergenic Biomarkers in the Molecular Diagnosis of IgE-Mediated Wheat Allergy
by Mariana Preda, Florin-Dan Popescu, Emilia Vassilopoulou and Sylwia Smolinska
Int. J. Mol. Sci. 2024, 25(15), 8210; https://doi.org/10.3390/ijms25158210 - 27 Jul 2024
Cited by 8 | Viewed by 4897
Abstract
IgE-mediated wheat allergy can take on various forms, including childhood food allergy to wheat, wheat-dependent exercise-induced anaphylaxis in young adults, baker’s respiratory allergy/asthma in workers exposed to wheat flour inhalation, and contact urticaria that is caused by hydrolyzed wheat proteins in some cosmetics, [...] Read more.
IgE-mediated wheat allergy can take on various forms, including childhood food allergy to wheat, wheat-dependent exercise-induced anaphylaxis in young adults, baker’s respiratory allergy/asthma in workers exposed to wheat flour inhalation, and contact urticaria that is caused by hydrolyzed wheat proteins in some cosmetics, and that is sometimes associated with a food allergy. Singleplex and multiplex immunoassays detect specific IgE antibodies to wheat allergenic molecular biomarkers such as omega-5 gliadin Tri a 19, lipid transfer protein Tri a 14, and alpha-amylase inhibitors. The fluorescence enzyme immunoassay with capsulated cellulose polymer solid-phase coupled allergens is a commonly used singleplex assay. Multiplex methods include the ELISA-based macroarray immunoassay using nano-bead technology and a microarray immunoassay on polymer-coated slides. Another promising diagnostic tool is the basophil activation test performed with omega-5 gliadin and other wheat protein types. Detailed comprehension of the structural and immunological features of the numerous wheat allergens significant in clinical settings is imperative for advancing diagnostic biomarkers for IgE-mediated wheat allergies. Full article
(This article belongs to the Special Issue Recent Advances in Gluten-Related Disorders)
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14 pages, 2219 KB  
Article
Comparative Characterization of Grain Protein Content and Composition by Chromatography-Based Separation Methods (SE-HPLC and RP-HPLC) of Ten Wheat Varieties Grown in Different Agro-Ecological Zones of Algeria
by Nesrine Hacini, Radia Djelloul, Ahmed Hadef, Marie-Françoise Samson and Dominique Desclaux
Separations 2022, 9(12), 443; https://doi.org/10.3390/separations9120443 - 15 Dec 2022
Cited by 5 | Viewed by 4128
Abstract
To characterize and compare the protein quality of ten durum wheat genotypes grown under three cropping modalities in Algeria (subhumid in Algiers, subhumid-semiarid in Constantine, and semiarid in Sétif), the protein profile of their kernels was performed by High-Performance Liquid Chromatography (SE-HPLC and [...] Read more.
To characterize and compare the protein quality of ten durum wheat genotypes grown under three cropping modalities in Algeria (subhumid in Algiers, subhumid-semiarid in Constantine, and semiarid in Sétif), the protein profile of their kernels was performed by High-Performance Liquid Chromatography (SE-HPLC and RP-HPLC). The “variety” factor has a major impact, mainly on the insoluble fraction (Fi), on the gliadin/glutenin ratio, on the large and small glutenin aggregates (F1 and F2, respectively), and on ω-gliadins and high molecular weight albumins (F3). Conversely, the total protein content and the albumin-globulin fraction (F5) depend mainly on the environment. The α- β- and γ-gliadins (F4) are equally dependent on variety and environment. The subhumid-semiarid agroecological conditions of Constantine (SH-SA) favored an important accumulation of proteins (14.1%), particularly by an increased synthesis of omega gliadins and high-molecular-weight glutenin subunits (HMW-GS), compared to those of Algiers (SH) and Sétif (SA). For these latter environments, metabolic-type proteins are predominant, reflected in a higher F5 fraction (p < 0.05) (albumin and globulin), and significantly more alpha-beta and gamma gliadins. The use of chromatographic analyses to characterize wheat genotypes remains a reliable tool for breeding and variety promotion programs and can provide a better understanding of the ecophysiology of cereal crops. Full article
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15 pages, 3117 KB  
Article
Response of Wheat Storage Proteins and Breadmaking Quality to Dimethylpyrazole-Based Nitrification Inhibitors under Different Nitrogen Fertilization Splitting Strategies
by Ximena Huérfano, José-María Estavillo, Miren K. Duñabeitia, María-Begoña González-Moro, Carmen González-Murua and Teresa Fuertes-Mendizábal
Plants 2021, 10(4), 703; https://doi.org/10.3390/plants10040703 - 6 Apr 2021
Cited by 2 | Viewed by 2799
Abstract
Improving fertilizer nitrogen (N) use efficiency is essential to increase crop productivity and avoid environmental damage. This study was conducted during four crop cycles of winter wheat under humid Mediterranean conditions (Araba, northern Spain). The effects of N-fertilization splitting and the application of [...] Read more.
Improving fertilizer nitrogen (N) use efficiency is essential to increase crop productivity and avoid environmental damage. This study was conducted during four crop cycles of winter wheat under humid Mediterranean conditions (Araba, northern Spain). The effects of N-fertilization splitting and the application of the nitrification inhibitors (NIs) 3,4-dimethylpyrazole phosphate (DMPP) and 2-(3,4-dimethyl-1H-pyrazol-1-yl) succinic acid isomeric mixture (DMPSA) as strategies to improve grain quality were examined. The hypothesis of this study was to test if the partial ammonium nutrition and the reduction of fertilizer losses presumably induced by the application of NIs can modify the grain gliadin and glutenin protein contents and the breadmaking quality (dough rheological properties). Among both NIs assayed, only DMPP showed a slight effect of decreasing the omega gliadin fraction, following splitting either two or three times, although this effect was dependent on the year and was not reflected in terms of dough extensibility. The slight decreases observed in grain quality in terms of dough strength and glutenin content induced by DMPP suggest that DMPSA is more promising in terms of maintaining grain quality. Nonetheless, these poor effects exerted by NI application on grain quality parameters did not lead to changes in the quality parameters defining the flour aptitudes for breadmaking. Full article
(This article belongs to the Special Issue Cereal Physiology and Breeding)
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14 pages, 2792 KB  
Article
Changes in Protein Non-Covalent Bonds and Aggregate Size during Dough Formation
by Sonoo Iwaki, Shiro Aono, Katsuyuki Hayakawa, Bin Xiao Fu and Chikako Otobe
Foods 2020, 9(11), 1643; https://doi.org/10.3390/foods9111643 - 11 Nov 2020
Cited by 31 | Viewed by 3853
Abstract
This research investigated changes in the amounts and sizes of monomeric proteins and protein aggregates during dough mixing, with a focus on the contribution of non-covalent bonds in the aggregation of gluten proteins. High protein flour (HF) and low protein flour (LF) were [...] Read more.
This research investigated changes in the amounts and sizes of monomeric proteins and protein aggregates during dough mixing, with a focus on the contribution of non-covalent bonds in the aggregation of gluten proteins. High protein flour (HF) and low protein flour (LF) were used in this study. As dough mixing progressed from flour to overmixed dough, the total amount of protein aggregates increased while the amount of monomeric protein decreased. Omega-gliadin was the major monomeric protein that decreased in quantity. Interestingly, the amount of larger-sized protein aggregates decreased and that of smaller-sized protein aggregates increased. The amount of gluten protein macro-polymer aggregated through strong non-covalent bonds decreased whereas aggregates formed with weaker non-covalent bonds increased. LF dough behaved similar to HF dough. Large-sized gluten protein aggregates disaggregated due to the weakening of non-covalent bonds and became smaller. Omega-gliadin was incorporated into gluten protein aggregates during dough mixing. Full article
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