Cited by 145Food Allergy and Anaphylaxis ResearchDrug-Induced Adverse ReactionsAllergic Rhinitis and Sensitization

Mechanisms underlying differential food allergy response to heated egg

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Martos, Gustavo, Lopez-Exposito, Ivan, Bencharitiwong, Ramon, Berin, M. Cecilia, Nowak-Węgrzyn, Anna·2011·Journal of Allergy and Clinical Immunology

Abstract

Background Egg white proteins are usually subjected to heating, making them edible for the majority of children with egg allergy. Objective We sought to investigate the underlying mechanisms responsible for the reduced allergenicity displayed by heat-treated egg white allergens. Methods C3H/HeJ mice were orally sensitized with ovalbumin (OVA) or ovomucoid and challenged with native or heated proteins to evaluate their allergenicity. Immunoreactivity was assessed by immunoblotting using sera from children with egg allergy. In vitro gastrointestinal digestion of native and heated OVA and ovomucoid was studied by SDS-PAGE and liquid chromatography. Intestinal uptake of intact native and heated OVA and ovomucoid by human intestinal epithelial (Caco-2) cells was investigated. Rat basophil leukemia cells passively sensitized with mouse serum and human basophils passively sensitized with serum from children with egg allergy were used to assess the effector cell activation by heated, digested, and transported OVA and ovomucoid. Results Heated OVA and ovomucoid did not induce symptoms of anaphylaxis in sensitized mice when administered orally. Heating did not completely destroy IgE-binding capacity of OVA or ovomucoid but enhanced in vitro digestibility of OVA. Digestion of both OVA and ovomucoid diminished mediator release in rat basophil leukemia assay and basophil activation. Heating of allergens prevented transport across human intestinal epithelial cells in a form capable of triggering basophil activation or T-cell activation. Conclusion Heat treatment reduces allergenicity of OVA and ovomucoid. This is partially a result of the enhanced gastrointestinal digestibility of heated OVA and the inability of heated OVA or ovomucoid to be absorbed in a form capable of triggering basophils.

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Authors
Martos, G., Lopez-Exposito, I., Bencharitiwong, R., Berin, M. C., & Nowak-Węgrzyn, A.
Affiliations
  • Instituto de Investigación en Ciencias de la Alimentación (ES)
  • Icahn School of Medicine at Mount Sinai (US)
Venue
Journal of Allergy and Clinical Immunology
Publisher
Elsevier BV
Published
2011-04
Volume
127
Issue
4
Pages
990-997.e2
ISSN
0091-6749 (ISSN-L)
OpenAlex
W2006204681
Cited by
145
References
2
Citations by year
2026: 1 · 2025: 5 · 2024: 5 · 2023: 6 · 2022: 6 · 2021: 6 · 2020: 8 · 2019: 5 · 2018: 7 · 2017: 10 · 2016: 9 · 2015: 21 · 2014: 19 · 2013: 15 · 2012: 17
FWCI
13.46
Type
journal article
Language
en
Open access
Locations
  • Journal of Allergy and Clinical Immunology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
Funders
  • National Institute of Allergy and Infectious Diseases (K23AI059318, U19AI044236, P01AI044236)
  • National Center for Research Resources (UL1RR029887)
Topics
  • Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
  • Health Sciences › Medicine › Pharmacology › Drug-Induced Adverse Reactions
  • Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
Keywords
egg allergy, ovalbumin, ovomucoid, allergenicity reduction, gastrointestinal digestion, intestinal absorption, basophil activation, IgE binding, T cell activation, oral tolerance, anaphylaxis
MeSH terms
Animals, Basophils, Chromatography, High Pressure Liquid, Cooking, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Female, Hot Temperature, Heating, Humans, Immunoglobulin E, Lymphocyte Activation, Ovalbumin, Ovomucin, T-Lymphocytes, Immunoblotting, Egg Hypersensitivity, Mice, Rats

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