Literature DB >> 32485264

Cow's milk protein β-lactoglobulin confers resilience against allergy by targeting complexed iron into immune cells.

Franziska Roth-Walter1, Sheriene Moussa Afify2, Luis F Pacios3, Bart R Blokhuis4, Frank Redegeld4, Andreas Regner5, Lisa-Marie Petje5, Alessandro Fiocchi6, Eva Untersmayr7, Zdenek Dvorak8, Karin Hufnagl9, Isabella Pali-Schöll9, Erika Jensen-Jarolim10.   

Abstract

BACKGROUND: Beta-lactoglobulin (BLG) is a bovine lipocalin in milk with an innate defense function. The circumstances under which BLG is associated with tolerance of or allergy to milk are not understood.
OBJECTIVE: Our aims were to assess the capacity of ligand-free apoBLG versus loaded BLG (holoBLG) to protect mice against allergy by using an iron-quercetin complex as an exemplary ligand and to study the molecular mechanisms of this protection.
METHODS: Binding of iron-quercetin to BLG was modeled and confirmed by spectroscopy and docking calculations. Serum IgE binding to apoBLG and holoBLG in children allergic to milk and children tolerant of milk was assessed. Mice were intranasally treated with apoBLG versus holoBLG and analyzed immunologically after systemic challenge. Aryl hydrocarbon receptor (AhR) activation was evaluated with reporter cells and Cyp1A1 expression. Treated human PBMCs and human mast cells were assessed by fluorescence-activated cell sorting and degranulation, respectively.
RESULTS: Modeling predicted masking of major IgE and T-cell epitopes of BLG by ligand binding. In line with this modeling, IgE binding in children allergic to milk was reduced toward holoBLG, which also impaired degranulation of mast cells. In mice, only treatments with holoBLG prevented allergic sensitization and anaphylaxis, while sustaining regulatory T cells. BLG facilitated quercetin-dependent AhR activation and, downstream of AhR, lung Cyp1A1 expression. HoloBLG shuttled iron into monocytic cells and impaired their antigen presentation.
CONCLUSION: The cargo of holoBLG is decisive in preventing allergy in vivo. BLG without cargo acted as an allergen in vivo and further primed human mast cells for degranulation in an antigen-independent fashion. Our data provide a mechanistic explanation why the same proteins can act either as tolerogens or as allergens.
Copyright © 2020. Published by Elsevier Inc.

Entities:  

Keywords:  Allergen; BLG; Bos d 5; allergy; cow's milk; iron; ligand; lipocalin; milk; quercetin; tolerance; β-lactoglobulin

Mesh:

Substances:

Year:  2020        PMID: 32485264     DOI: 10.1016/j.jaci.2020.05.023

Source DB:  PubMed          Journal:  J Allergy Clin Immunol        ISSN: 0091-6749            Impact factor:   10.793


  12 in total

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Authors:  Sheriene Moussa Afify; Isabella Pali-Schöll; Karin Hufnagl; Gerlinde Hofstetter; Maha Abdel-Rafea El-Bassuoni; Franziska Roth-Walter; Erika Jensen-Jarolim
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10.  Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines update - III - Cow's milk allergens and mechanisms triggering immune activation.

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Journal:  World Allergy Organ J       Date:  2022-09-15       Impact factor: 5.516

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