Characterization of IgE and IgG Epitopes on Ovomucoid Using Egg-White-Allergic Patients' Sera
Abstract
To investigate the importance of linear and conformational structure and carbohydrate chains in hen ovomucoid epitopes, the IgG and IgE binding activities of three native and reduced carboxymethylated (RCM) domains (DI, DII, and DIII) were compared using human sera from egg-white-allergic patients. There was significantly more IgG and IgE binding activity to DIII than to DI and DII. The IgG binding activity to RCM domains was similar to the native form, while RCM-DIII had significantly greater binding activity to IgE antibody (p < 0.05). It indicated that the main IgE and IgG epitopes on each domain were of linear structure. However, the total reactivity of the three domains was estimated to be about 50-60% (IgG binding) and 55-75% (IgE binding) compared with total reactivity in ovomucoid, resulting in some ovomucoid epitopes consisting of conformational epitopes on domain I-II or II-III. The carbohydrate moieties in DIII had a rather inhibiting effect on its IgG and IgE binding activities.
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The immunoreactive fragments obtained after duodenal digestion of glycosylated and deglycosylated ovomucoid were totally or partially coincident with previously described epitopes.
“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 [7]
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Recent advances in the understanding of egg allergens: basic, industrial, and clinical perspectives
Mine, Y., & Yang, M. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8001153 · Cited by 196 · see citing works
Self-citationHolen, E., Bolann, B., & Elsayed, S. (2001) · Clinical & Experimental Allergy · doi:10.1046/j.1365-2222.2001.01102.x · Cited by 76 · see citing works
Benedé, S., López-Fandiño, R., Reche, M., Molina, E., & López-Expósito, I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080810 · Cited by 33 · see citing works
“Most of these high-frequency IgE-binding peptides were either totally or partially coincident with previously described epitopes [5,7,25,28,32,33].”
BackgroundInfluential
- Authors
- Zhang, J. W., & Mine, Y.
- Affiliations
- University of Guelph (CA)
- Corresponding author
- Mine, Yoshinori
- ORCID
- Mine, Yoshinori
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1998-12
- Volume
- 253
- Issue
- 1
- Pages
- 124-127
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1975184227
- Cited by
- 55
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 1
- FWCI
- 0.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- ovomucoid, egg white allergy, IgE epitopes, linear epitopes, conformational epitopes, carbohydrate moiety, ovalbumin
- MeSH terms
- Allergens, Epitopes, Binding Sites, Antibody, Carbohydrates, Child, Preschool, Egg White, Enzyme-Linked Immunosorbent Assay, Food Hypersensitivity, Humans, Immunoglobulin E, Immunoglobulin G, Infant, Ovomucin, Peptide Fragments, Protein Conformation, Carbohydrate Metabolism
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