Enhanced uptake of processed bovine β‐lactoglobulin by antigen presenting cells: Identification of receptors and implications for allergenicity

SCOPE β-lactoglobulin (BLG) is a major cow milk allergen encountered by the immune system of infants fed with milk-based formulas. To determine the effect of processing on immunogenicity of BLG, we characterised how heated and glycated BLG are recognised and internalised by APCs. Also, the effect of heat-induced structural changes as well as gastrointestinal digestion on immunogenicity of BLG was evaluated. METHODS AND RESULTS The binding and uptake of BLG from raw cow milk and heated either alone (BLG-H) or with lactose/glucose (BLG-Lac and BLG-Glu) to the receptors present on APCs were analysed by ELISA and cell-binding assays. Heated and glycated BLG was internalised via Gal-3, CD36, and SR-AI while binding to RAGE did not cause internalization. CONCLUSIONS This study defines structural characteristics of heated and glycated BLG determining its' interaction with APCs via specific receptors thus revealing enhanced immunogenicity of glycated BLG versus heated. This article is protected by copyright. All rights reserved.