ArticleMolecular nutrition & food research2021
Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity.
Article in Molecular nutrition & food research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Exploring Siglecs: Potential Modulators of Immune Cells in Food Allergy and Therapeutic Applications.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2025Review
- Main Processed Hypoallergenic Foods: A Potential Tool to Improve Informed Dietary Choices in Children with IgE-Mediated Food Allergies.Children (Basel, Switzerland) · 2025Review
- Functional Characterization of Glycated Peptide Aggregates in Whey Protein Hydrolysates.Food science & nutrition · 2025Article
- Diabetic Glycation of Human Serum Albumin Affects Its Immunogenicity.Biomolecules · 2024Article
- Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines update - III - Cow's milk allergens and mechanisms triggering immune activation.The World Allergy Organization journal · 2022Article
- Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy.Nutrients · 2022Review
- No Glycation Required: Interference of Casein in AGE Receptor Binding Tests.Foods (Basel, Switzerland) · 2021Article
- Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity.Molecular nutrition & food research · 2021Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
scopeβ-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, this article characterized how heated and glycated BLG are recognized and internalized by APCs. Also, the effect of heat-induced structural changes as well as gastrointestinal digestion on immunogenicity of BLG is evaluated. METHODS AND
resultsThe 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 are analyzed by ELISA and cell-binding assays. Heated and glycated BLG is internalized via galectin-3 (Gal-3)and scavenger receptors (CD36 and SR-AI) while binding to the receptor for advanced glycation end products (R AGE) does not cause internalization. Receptor affinity of BLG is dependent on increased hydrophobicity, β-sheet exposure and aggregation. Digested glycated BLG maintained binding to sRAGE and Gal-3 but not to CD36 and SR-AI, and is detected on the surface of APCs. This suggests a mechanism via which digested glycated BLG may trigger innate (via RAGE) and adaptive immunity (via Gal-3).
conclusionsThis study defines structural characteristics of heated and glycated BLG determining its interaction with APCs via specific receptors thus revealing enhanced immunogenicity of glycated versus heated BLG.
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