Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells
| العنوان: | Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells |
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| المؤلفون: | Huub F. J. Savelkoul, R. J. Joost van Neerven, Nicolette W. de Jong, Kasper Hettinga, Harry J. Wichers, Malgorzata Teodorowicz, Sabrina Gensberger-Reigl, Theodoros Tsallis, Andreas Mauser, Hannah E. Zenker, Arifa Ewaz |
| المساهمون: | Internal Medicine |
| المصدر: | Molecular Nutrition and Food Research 65 (2021) 8 Molecular Nutrition and Food Research, 65(8) Molecular Nutrition & Food Research Molecular Nutrition and Food Research, 65(8):2000834. Wiley-VCH |
| بيانات النشر: | Wiley-VCH, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | CD36 Antigens, 0301 basic medicine, Food Handling, Lactoglobulins, RAGE (receptor), Glycation, cow milk processing, Internalization, Receptor, Research Articles, media_common, Chemistry, Immunogenicity, Scavenger Receptors, Class A, Blood Proteins, Endocytosis, Health & Consumer Research, Milk, Food Quality and Design, Biochemistry, Digestion, Mitogen-Activated Protein Kinases, Research Article, Biotechnology, Galectins, media_common.quotation_subject, Antigen-Presenting Cells, Celbiologie en Immunologie, digestion of β-lactoglobulin, 03 medical and health sciences, Immune system, Antigens, Neoplasm, Animals, Humans, Scavenger receptor, galactin-3 Maillard reaction ligands, Antigen-presenting cell, Food Process Engineering, galactin‐3 Maillard reaction ligands, VLAG, Food, Health & Consumer Research, glycation of β‐lactoglobulin, 030109 nutrition & dietetics, Macrophages, Infant, aggregation of β‐lactoglobulin, 030104 developmental biology, digestion of β‐lactoglobulin, Cell Biology and Immunology, Food, WIAS, aggregation of β-lactoglobulin, glycation of β-lactoglobulin, RAGE Maillard reaction ligands, Milk Hypersensitivity, Food Science |
| الوصف: | 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, 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 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 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). 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 versus heated BLG. Heat treatment of bovine milk antigen bovine β‐lactoglobulin (BLG) generates ligands for RAGE, Gal‐3, CD‐36 and SR‐AI as a result of structural changes and glycation. Glycated BLG is less sensitive to digestion and maintains its binding to RAGE and Gal‐3. Post‐digestion retained immunogenicity of glycated BLG may be mediated via RAGE as a signaling pathway, and via Gal‐3 facilitating internalization. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1613-4133 1613-4125 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::252703e7ee9aea6bfaa5565241510c2dTest https://doi.org/10.1002/mnfr.202000834Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....252703e7ee9aea6bfaa5565241510c2d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16134133 16134125 |
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