Identification and fine mapping of IgG and IgE epitopes in ovomucoid.

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.

• 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)
• Copyright: (c)2002 Elsevier Science (USA).

Chemical References

• Epitopes
• Immunoglobulin G
• Peptide Library
• Ovomucin
• Immunoglobulin E

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