Year: 1999
Type: dissertation
Abstract: Ovomucoid, the major allergen in egg white, contains DI, DII, and DIII-CHO+ or DIII-CHO$-$. There was significantly more IgG binding to DIII and significantly more IgE binding to DIII-CHO$-$ than to either DI or DII. The main IgE and IgG epitopes on each domain were linear. The carbohydrate moiety in DIII had a rather inhibiting effect on its IgG binding and no effect on its IgE binding activities. Three IgE epitopes (EE1 and EE2, 159-173; EE3, 179-186) and three IgG epitopes (EG1, 161-167; EG2, 165-174; EG3, 177-183) were identified. The critical amino acids for IgE epitopes were Y$\sp{161}$, G$\sp{162}$, N$\sp{163}$, F$\sp{167}$, C$\sp{168}$, A$\sp{170}$ and/or K$\sp{185}$, C$\sp{186}$ and for IgG were from K$\sp{164}$ to C$\sp{168}$ and from T$\sp{177}$ to H$\sp{182}$. A hydrophobic amino acid group may be more critical for IgE binding to DIII, whereas a hydrophilic amino acid group appears to be more critical for IgG binding.
Author: Zhang, Jie Wei
Language: English
Subfield: Immunology and Allergy
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W7048162461