Wheat is a prominent allergenic food that can trigger life-threatening anaphylaxis. Presently, it remains unclear whether wheat glutenin (WG) extract possesses inherent sensitization potential independently, without the use of adjuvants, and whether it can sensitize mice to the extent of inducing life-threatening systemic anaphylaxis. In this study, we tested the hypothesis that repeated skin exposures to WG extract without adjuvant will sensitize mice with the resultant anaphylactic reaction upon systemic WG challenge. Balb/c mice were bred and maintained on a strict plant protein-free diet and were repeatedly exposed to a WG extract or vehicle once a week for 9 weeks. WG-specific (s)IgE and total (t)IgE levels were quantified. Mice were challenged with WG extract to induce anaphylactic reactions as measured by hypothermic shock response (HSR) and mucosal mast cell degranulation response (MMCR). We also conducted proteomic analysis of 120 spleen immune markers. These skin-sensitized mice exhibited exposure-dependent IgE responses and near-fatal anaphylaxis upon challenge. Proteomic analysis identified seven dramatically elevated immune biomarkers in anaphylactic mice. These data reveal that WG is intrinsically allergenic, and that chronic skin exposure to WG extract can prime the mice for potentially fatal anaphylaxis.
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http://dx.doi.org/10.3390/ijms242417247 | DOI Listing |
Int J Biol Macromol
January 2025
College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China. Electronic address:
To elucidate the effect of transglutaminase (TG) on the rheological properties of wheat gluten, this study investigates the underlying mechanisms by analyzing changes in gluten structure. The results demonstrated that the TG-treated gluten samples had higher storage modulus (G') and loss modulus (G″) compared to the control, conversely, creep and recovery strains followed an opposite trend. Notably, the most pronounced effects were observed with adding 2 U/g TG for 20-30 min.
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
Department of Plant Breeding, Swedish University of Agricultural Sciences, Box 190, Lomma SE-23422, Sweden.
In this study, the impact of the varying environments, wet-cool (2017), dry-hot (2018), and fluctuating (2019), on two spring wheat genotypes, Diskett and Bumble, grown in field conditions in southern Sweden was studied. From harvested grains, polymeric gluten proteins were fractionated and collected using SE-HPLC and then analyzed with LC-MS/MS. Proteins and peptides identified through searches against the protein sequences of (taxon 4565) from the UniProtKB database showed 7 high molecular weight glutenin subunits (HMW-GS) and 24 low molecular weight glutenin subunits (LMW-GS) with different enrichment levels for both genotypes.
View Article and Find Full Text PDFACS Omega
December 2024
Graduate Institute of Biomedical Optomechatronics, Taipei Medical University, Taipei 110, Taiwan.
In recent years, food allergies and food sensitivities have remained critical public health problems that affect approximately 15% of the global population. Wheat is a major food source worldwide, but it is also a common food allergen. Celiac disease is chronic immune-mediated enteropathy triggered by exposure to dietary gluten in genetically predisposed individuals; it can be treated only through strict gluten avoidance.
View Article and Find Full Text PDFJ Sci Food Agric
December 2024
Department of Food Science and Engineering, Institute of Food Safety and Nutrition, Jinan University, Guangzhou, China.
Background: Wheat gluten (WG) is a crucial cereal protein commonly utilized in the food, biological and pharmaceutical industries. However, WG is poorly soluble in water, resulting in poor functional properties, which restrict its application in the food industry. As a result, there is an urgent need for improving the properties of WG.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
College of Food Science and Engineering, Gansu Agricultural University, Lanzhou 730070, Gansu, People's Republic of China; State Key Laboratory of Aridland Crop Science, Lanzhou 730070, Gansu, People's Republic of China. Electronic address:
Our previous study found that pectin with different degrees of esterification (DE) could affect the thermal aggregation of gluten, but the mechanism was not clear. Analyzing the thermal aggregation of glutenin and gliadin supplemented with pectin can clarify this mechanism. With the increase of temperature, the particle size, disulfide bonds and β-sheet of glutenins increased, the surface hydrophobicity (H) and fluorescence intensity decreased, and the network gradually aggregated, but the change trend of gliadins was opposite.
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