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Allergenic properties of ovomucoid in man
Abstract
Ovomucoid, the dominant allergen in hen’s egg, is a highly glycosylated protein comprising 186 amino acids arranged in three tandem domains (Gal d 1.1, 1.2, and 1.3). The purpose of this study was to evaluate the allergenic properties of ovomucoid. The three ovomucoid domains were isolated and evaluated with sera from egg allergic patients to determine B cell domain specificity, B cell epitopes, and the relative importance of linear and conformational structures and carbohydrate chains to B cell epitopes. Peripheral blood T cells from egg allergic patients were used to evaluate T-dominant domains and reactivity to reduced and oxidized ovomucoid. There was significantly more IgE activity to the second ovomucoid domain (median percentage of ovomucoid-specific IgE: Gal d 1.2, 40%; Gal d 1.1, 23%; Gal d 1.3, 26%). Quantities of patient IgG Ab were comparable for all three domains. Five IgE and seven IgG binding regions were identified. IgE Ab binding to reduced ovomucoid and IgG binding to oxidized ovomucoid were significantly reduced compared with that to native ovomucoid (28 and 69%, respectively). Peripheral blood T cells of 21 of 33 patients reacted to Gal d 1.3, 18 of 33 reacted to Gal d 1.2, and 18 of 33 reacted to Gal d 1.1. T cell proliferation in vitro in response to reduced and oxidized ovomucoid were significantly greater than that in response to the native protein. These results indicate a dichotomy between T and B cell domain dominance, and the presence of both unique and common IgE and IgG epitopes. Furthermore, the results suggest that conformational B cell epitopes play a more significant role in ovomucoid allergenicity than previously appreciated, and that carbohydrate moieties have a minor effect on allergenicity.
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“both, OM and dOM, yielded, after the duodenal phase, immunoreactive fragments that were totally or partially coincident with previously described epitopes.”
From Influence of the Carbohydrate Moieties on the Immunoreactivity and Digestibility of the Egg Allergen Ovomucoid (2013) · cites this paper as [5]
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Metadata
- Authors
- Cooke, S. K., & Sampson, H. A.
- Affiliations
- Johns Hopkins University (US)
- ORCID
- Sampson, H A
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 1997-08
- Volume
- 159
- Issue
- 4
- Pages
- 2026-2032
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W1559185201
- Cited by
- 250
- References
- 0
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 1 · 2023: 9 · 2022: 2 · 2021: 9 · 2020: 6 · 2019: 7 · 2018: 11 · 2017: 3 · 2016: 8 · 2015: 12 · 2014: 16 · 2013: 14 · 2012: 15
- FWCI
- 1.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (7r01ai024439-11)
- National Institute of Allergy and Infectious Diseases (AI 24439)
- National Center for Research Resources (RR 000 52)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Health Sciences › Medicine › Pharmacology (medical) › Drug-Induced Adverse Reactions
- Keywords
- ovomucoid, egg allergy, B-cell epitopes, conformational epitopes, IgE binding, IgG binding, T cell proliferation, protein glycosylation, oxidized proteins, reduced protein
- MeSH terms
- Allergens, Amino Acid Sequence, Child, Food Hypersensitivity, Humans, Immunoglobulin E, Molecular Sequence Data, Ovomucin, T-Lymphocytes
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