Abstract |
Ovomucoid is a major allergen in hen egg white which causes a serious IgE-mediated food allergy reaction. This study determined eight IgG epitopes, 5-11 amino acids in length, and nine IgE epitopes, 5-16 amino acids in length, within the primary sequence in ovomucoid using arrays of overlapping peptides synthesized on cellulose membranes. Pooled sera from eight egg-allergic patients were used to probe the membrane. We also analyzed the amino acids that are critical for antibody binding by substituting a single amino acid within each epitope. Mutational analysis of the epitopes indicated that charged amino acids ( aspartic acid, glutamic acid, and lysine) and some hydrophobic ( leucine, phenylalanine, and glycine) and polar ( serine, threonine, tyrosine, and cystein) amino acids were important for antibody binding. These results provide useful information for the molecular design necessary to reduce the allergenicity of ovomucoid, and a better understanding of structure-function relationships of allergic epitopes in food proteins.
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Authors | Yoshinori Mine, Jie Wei Zhang |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 292
Issue 4
Pg. 1070-4
(Apr 12 2002)
ISSN: 0006-291X [Print] United States |
PMID | 11944924
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | (c)2002 Elsevier Science (USA). |
Chemical References |
- Epitopes
- Immunoglobulin G
- Peptide Library
- Ovomucin
- Immunoglobulin E
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Topics |
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Chickens
- Egg Hypersensitivity
(immunology)
- Epitope Mapping
- Epitopes
(chemistry, immunology, metabolism)
- Humans
- Immunoglobulin E
(metabolism)
- Immunoglobulin G
(metabolism)
- Molecular Sequence Data
- Ovomucin
(chemistry, immunology, metabolism)
- Peptide Library
- Structure-Activity Relationship
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