AI Article Synopsis
- β-lactoglobulin (BLG) is a significant allergen in cow milk that affects infants consuming milk-based formulas, and this study examines how processing methods influence its immunogenicity.
- The research analyzes how different forms of BLG, including raw, heated, and glycated versions, interact with antigen-presenting cells (APCs) and highlights the receptors involved in their internalization.
- Findings indicate that glycated BLG has a higher immunogenic potential compared to heated BLG, as it interacts with specific receptors on APCs that could trigger both innate and adaptive immune responses.
Article Abstract
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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8244112 | PMC |
| http://dx.doi.org/10.1002/mnfr.202000834 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Functional improvements in β-lactoglobulin by conjugation with high methoxy pectin by the Maillard reaction.
Cytotechnology
February 2025
Department of Applied Biological Science, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-Cho, Fuchu, Tokyo 183-8509 Japan.
β-lactoglobulin (BLG), a major protein in whey, was conjugated with high methoxy pectin (HMP) by the Maillard reaction to improve emulsifying property and reduce allergenicity of BLG. The Maillard reaction was carried out at a weight ratio BLG: HMP = 1:4.15 and 1:6 at 60 °C at a relative humidity of 79% for 5 days.
View Article and Find Full Text PDFAllergenicity assessment of β-lactoglobulin ferulic acid-glucose conjugates.
Food Chem
December 2024
College of Life Science, National R&D Center for Freshwater Fish Processing, Jiangxi Normal University, Nanchang, Jiangxi 330022, China. Electronic address:
We prepared the β-lactoglobulin (BLG)-ferulic acid (FA)-glucose (Glu) conjugates by alkaline method and Maillard reaction to assess the allergenicity. FA and Glu can form a ternary covalent conjugate with BLG, as evidenced by the shortening of SEC retention time, upward migration of SDS-PAGE protein bands, considerable decrease in free amino and sulfhydryl content, and changes in multistructure. BLG-Glu-FA conjugates weakly bound to immunoglobulin E in allergic sera was weak, reduced interleukin 4 and tumor necrosis factor α levels in RBL-2H3 cells and histamin and interleukin 6 secretion levels in KU812 cells, and inhibited the nuclear factor-κB signaling pathway.
View Article and Find Full Text PDFThe effect of B-type procyanidin on free radical and metal ion induced β-lactoglobulin glyco-oxidation via mass spectrometry and interaction analysis.
Food Res Int
June 2023
College of Food Science, Shenyang Agricultural University, Shenyang 100866, China. Electronic address:
Procyanidin is a group of dietary flavonoids abundant in berry fruits. In this study, the effects and underlying mechanisms of B type procyanidin (PC) on free radical and metal ion (HO, AAPH and Fe) induced milk protein β-lactoglobulin (BLG) glyco-oxidation were investigated. The results indicated that PC protected BLG structure changes from cross-link and aggregation induced by free radicals and metal ion.
View Article and Find Full Text PDFReduced immunogenicity and endowed antimicrobial activity in β-lactoglobulin by preparing edible bioconjugate.
Cytotechnology
February 2023
Department of Applied Biological Science, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-Cho, Fuchu, Tokyo 183-8509 Japan.
β-lactoglobulin (BLG) and ε-polylysine (PL) were bound by using microbial transglutaminase. Dextran (Dex) was further conjugated to the BLG-PL conjugate by the Maillard reaction. Confirmation of conjugation was carried out by SDS-PAGE.
View Article and Find Full Text PDFEffect of pH on the interfacial and foaming properties of Maillard reaction-modified proteins.
Biophys Chem
December 2022
Department of Chemical Engineering, Faculty of Chemistry, Universidad de Sevilla, Prof. García González 1, 41012 Sevilla, Spain.
The interfacial and foaming properties of two conjugates obtained by Maillard reaction was determinate, at heating times of 36 and 60 h. The effect of covalent interaction between β-lactoglobulin (β-Lg) and two dextran molecular weights (10 and 20 kDa) were evaluated at pH 7 and pH 5, establishing protein controls, mixed systems, and mixing controls for each system. At pH 7, the first conjugate showed an increase in surface activity, while the other showed an opposite effect on the glycosylation process.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!