Cow’s milk protein β-lactoglobulin confers resilience against allergy by targeting complexed iron into immune cells
نویسندگان
چکیده
BackgroundBeta-lactoglobulin (BLG) is a bovine lipocalin in milk with an innate defense function. The circumstances under which BLG associated tolerance of or allergy to are not understood.ObjectiveOur aims were assess the capacity ligand-free apoBLG versus loaded (holoBLG) protect mice against by using iron-quercetin complex as exemplary ligand and study molecular mechanisms this protection.MethodsBinding was modeled confirmed spectroscopy docking calculations. Serum IgE binding holoBLG children allergic tolerant assessed. Mice intranasally treated analyzed immunologically after systemic challenge. Aryl hydrocarbon receptor (AhR) activation evaluated reporter cells Cyp1A1 expression. Treated human PBMCs mast assessed fluorescence-activated cell sorting degranulation, respectively.ResultsModeling predicted masking major T-cell epitopes binding. In line modeling, reduced toward holoBLG, also impaired degranulation cells. mice, only treatments prevented sensitization anaphylaxis, while sustaining regulatory T facilitated quercetin-dependent AhR and, downstream AhR, lung HoloBLG shuttled iron into monocytic their antigen presentation.ConclusionThe cargo decisive preventing vivo. without acted allergen vivo further primed for antigen-independent fashion. Our data provide mechanistic explanation why same proteins can act either tolerogens allergens. Beta-lactoglobulin understood. protection. Binding respectively. Modeling presentation.
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ژورنال
عنوان ژورنال: The Journal of Allergy and Clinical Immunology
سال: 2021
ISSN: ['1097-6825', '0091-6749', '1085-8725']
DOI: https://doi.org/10.1016/j.jaci.2020.05.023