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

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

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From the article: "Scope: During food processing, the Maillard reaction (
М R) 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 results: 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.
Conclusions: 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."

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OrganisatieHogeschool Utrecht
AfdelingKenniscentrum Gezond en Duurzaam Leven
LectoraatInnovative Testing in Life Sciences and Chemistry
Jaar2018
TypeArtikel
TaalEngels

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