Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Molecular Nutrition & Food Research
Marija PeruskoJoost Smit

Abstract

During 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. BLG 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+ T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. This study suggests that glycation of BLG by MR signi...Continue Reading

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Citations

Jan 8, 2021·Clinical Reviews in Allergy & Immunology·Joana CostaThomas Holzhauser
Dec 19, 2020·Comprehensive Reviews in Food Science and Food Safety·Qiaozhi ZhangLinglin Fu
Dec 10, 2019·Journal of Agricultural and Food Chemistry·Clélia VilleminGrégory Bouchaud

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Methods Mentioned

BETA
thermal treatment
ELISA
flow cytometry
FCS
confocal microscopy

Software Mentioned

CDPro package
GraphPad Prism
CONTIN
BD Accuri

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