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

Marija Perusko, Manon van Roest, Dragana Stanic‐Vucinic, Peter J. Simons, Raymond H. H. Pieters, Tanja Cirkovic Velickovic, Joost J. Smit

During food processing the Maillard reaction (МR) may occur resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergy since glycation may influence interactions with 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 significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy. This article is protected by copyright. All rights reserved.