ArticleMolecular nutrition & food research2018
Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.
Article in Molecular nutrition & food research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 58 citations in OpenAlex.
- Dietary advanced glycation end-products promote food allergy by disrupting intestinal barrier and enhancing Th2 immunity.Nature communications · 2025Article
- Coculture of Human Dendritic and T Cells for the Study of Specific T Cell-Mediated Responses Against Food Allergens.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Characterization of sow milk N-linked glycoproteome over the course of lactation.Journal of animal science · 2023Article
- Reduction in Allergenicity and Induction of Oral Tolerance of Glycated Tropomyosin from Crab.Molecules (Basel, Switzerland) · 2022Article
- Maillard Reaction Induced Changes in Allergenicity of Food.Foods (Basel, Switzerland) · 2022Review
- Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?Clinical reviews in allergy & immunology · 2022Review
- Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy.Nutrients · 2022Review
- Limited Lactosylation of Beta-Lactoglobulin from Cow's Milk Exerts Strong Influence on Antigenicity and Degranulation of Mast Cells.Nutrients · 2021Article
- Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity.Molecular nutrition & food research · 2021Article
- Article
- Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition.Nutrients · 2019Article
- Influence of the Maillard Reaction on the Allergenicity of Food Proteins and the Development of Allergic Inflammation.Current allergy and asthma reports · 2019Review
- Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.Molecular nutrition & food research · 2018Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 4 countries.
Funding
Abstract
scopeDuring food processing, the Maillard reaction (МR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen β-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. METHODS AND
resultsBLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4
conclusionsThis study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
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