1. Reducing the Allergenicity of β-Lactoglobulin by Covalent Modification with Different Contents of Epigallocatechin Gallate (EGCG): In Vitro and In Vivo Studies.
- Author
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Yue W, Huang S, Ye L, Fan Y, Chen J, Li L, and Wu X
- Subjects
- Animals, Cattle, Humans, Mice, Milk Hypersensitivity immunology, Milk Hypersensitivity prevention & control, Mice, Inbred BALB C, Female, Interferon-gamma immunology, Interferon-gamma metabolism, Chymases chemistry, Chymases immunology, Chymases metabolism, Th2 Cells immunology, Th2 Cells drug effects, Interleukin-5 immunology, Interleukin-10 immunology, Interleukin-10 metabolism, Interleukin-4 immunology, Interleukin-4 metabolism, Mast Cells immunology, Mast Cells drug effects, Lactoglobulins chemistry, Lactoglobulins immunology, Catechin analogs & derivatives, Catechin chemistry, Catechin immunology, Allergens immunology, Allergens chemistry, Immunoglobulin E immunology
- Abstract
β-Lactoglobulin (βLG) is a major allergen in bovine milk protein. This study was designed to investigate changes in βLG structure, digestibility, and allergenicity induced by covalent binding modification with different contents of (-)-epigallocatechin 3-gallate (EGCG). The reaction of EGCG conjugation with βLG reached saturation at a molar ratio of 1:60 βLG:EGCG. Conjugation with EGCG altered the βLG structure, decreased IgE-binding capacity, and increased digestibility in a dose-dependent manner. In vivo studies showed that covalent conjugation with EGCG can reduce βLG-induced allergic symptoms with reducing levels of IgE, histamine, and mast cell protease-1 (mMCP-1) and the percentage of sensitized mast cells. Allergenicity was reduced more effectively in saturated βLG-EGCG conjugates compared to semisaturated conjugates. Observed changes in IFN-γ, IL-4, IL-5, IL-10, and TGF-β levels suggested that βLG-EGCG conjugates were able to promote Th1/Th2 immune balance. These findings further our understanding of the relationship between the degree of polyphenol conjugation and the allergenicity of food allergens.
- Published
- 2024
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