Further characterization of IgE-binding antigens in horse dander, with particular emphasis on glycoprotein allergens.
Abstract: IgE-binding components in an extract of horse dander were analyzed, especially with regard to the glycoprotein allergens. After SDS-PAGE under reducing conditions and blotting, several of the glycoprotein IgE-binding components, including two distinct bands of 27 and 31 kDa, were detected. Together with several other bands, they were shown to bind to the lectins Sambucus nigra agglutinin (SNA) and Datura stramonium agglutinin (DSA), indicating terminal sialic acid linked alpha 2 --> 6 to galactose, and galactose linked beta 1 --> 4 to N-acetylglucosamine, respectively. Carbohydrate analysis after SDS-PAGE and blotting showed the presence of mannose, galactose, N-acetylglucosamine, and N-acetyl neuraminic acid in the 27-kDa band. The 14.4-kDa glycoprotein component lost its IgE-binding activity after periodate oxidation. Minor differences in allergenic activity in the other glycoprotein allergenic components were also detected, indicating that the carbohydrate part of the molecule seems to play a role in the IgE-binding activity. Two-dimensional electrophoresis and subsequent immunoblotting were performed to estimate the approximate number, molecular mass, and pI of IgE-binding components. This resulted in a cluster of such components on the blot membrane.
Publication Date: 1996-09-01 PubMed ID: 8899112DOI: 10.1111/j.1398-9995.1996.tb04680.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research focused on studying the components in horse dander that trigger allergies, placing special attention on glycoprotein allergens. Components that bind with Immunoglobulin E (IgE) were analyzed and found to include specific sized glycoprotein components. Notably, the study found evidence that the carbohydrate section of these molecules may influence their activity in triggering allergies.
Research Methodology
- The research used an extract of horse dander to analyze its IgE-binding components.
- The analysis was focused on glycoprotein allergens.
- SDS-PAGE, a method to separate proteins based on their size, and blotting, a technique to transfer DNA, RNA, and proteins onto a carrier, were used under reducing conditions.
Significant Findings
- Several glycoprotein IgE-binding components were detected.
- Two distinct bands of these components, sizing 27 and 31 kDa, were found.
- These bands, along with other bands, were shown to bind to specific lectins – proteins that bind to specific carbohydrates.
- The study also showed that these bands indicate particular links between sugar molecules.
- Carbohydrate analysis showed the presence of certain sugars in the 27-kDa band.
- The 14.4-kDa glycoprotein component lost its IgE-binding activity after oxidation with periodate, a reagent used to cleave carbon-carbon bonds.
Analyzing the Role of Carbohydrates in Allergenic Activity
- Subtle differences in allergenic activity were found in the other glycoprotein allergenic components.
- This points towards the carbohydrate part of the molecule having a role in the IgE-binding activity.
Additional Analysis
- Two-dimensional electrophoresis, a technique to separate complex mixtures of proteins, and subsequent immunoblotting were performed to estimate the approximate number, atomic mass, and pI (a measure of acidity or basicity) of IgE-binding components.
- These subsequent tests resulted in a cluster of such components on the blot membrane.
Cite This Article
APA
Johnsen , Thanh DB, Ly Q, Smestad Paulsen B, Wold JK.
(1996).
Further characterization of IgE-binding antigens in horse dander, with particular emphasis on glycoprotein allergens.
Allergy, 51(9), 608-613.
https://doi.org/10.1111/j.1398-9995.1996.tb04680.x Publication
Researcher Affiliations
- Department of Pharmacognosy, Institute of Pharmacy, University of Oslo, Norway.
MeSH Terms
- Allergens / analysis
- Allergens / immunology
- Animals
- Binding Sites, Antibody / immunology
- Electrophoresis, Gel, Two-Dimensional
- Glycoproteins / immunology
- Hair
- Horses
- Humans
- Immunoblotting
- Immunoglobulin E / immunology
- Lectins
Citations
This article has been cited 2 times.- Fötisch K, Vieths S. N- and O-linked oligosaccharides of allergenic glycoproteins. Glycoconj J 2001 May;18(5):373-90.
- Young M, Davies MJ, Bailey D, Gradwell MJ, Smestad-Paulsen B, Wold JK, Barnes RM, Hounsell EF. Characterization of oligosaccharides from an antigenic mannan of Saccharomyces cerevisiae. Glycoconj J 1998 Aug;15(8):815-22.
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