Serological, genomic and structural analyses of the major mite allergen Der p 23
| Autor: | Martin D. Chapman, Jill Glesner, Anna Pomés, Lalith Perera, Lori L. Edwards, Eugene F. DeRose, Geoffrey A. Mueller, Robert E. London, Lars C. Pedersen, Thomas A. Randall |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Models Molecular Protein Conformation Immunology Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Immunoglobulin E medicine.disease_cause Crystallography X-Ray Article Serology 03 medical and health sciences chemistry.chemical_compound Allergen Chitin Chitin binding medicine Mite Hypersensitivity Immunology and Allergy Animals Humans Amino Acid Sequence Antigens Dermatophagoides Nuclear Magnetic Resonance Biomolecular House dust mite biology Genomics Carbohydrate Allergens biology.organism_classification Molecular biology 030104 developmental biology chemistry biology.protein |
| Zdroj: | Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology. 46(2) |
| ISSN: | 1365-2222 |
| Popis: | Background Der p 23 was recently identified in a European population as a major allergen and potentially a chitin binding protein. Objective This study sought to assess the importance of Der p 23 among other Dermatophagoides allergens in a North American population and to determine the structure for functional characterization. Methods IgE binding to Der p 23, Der p 1, Der p 2, Der p 5, Der p 7 and Der p 8 was measured by ELISA. RNA-seq data from D. pteronyssinus were compared as estimates of allergen expression levels. The structure was analysed by X-ray crystallography and NMR. Results Despite a high prevalence of Der p 23, (75% vs. 87% and 79% for Der p 1 and Der p 2, respectively), the anti-Der p 23 IgE levels were relatively low. The patient response to the 6 allergens tested was variable (n = 47), but on average anti-Der p 1 and anti-Der p 2 together accounted for 85% of the specific IgE. In terms of abundance, the RNA expression level of Der p 23 is the lowest of the major allergens, thirty fold less than Der p 1 and sevenfold less than Der p 2. The structure of Der p 23 is a small, globular protein stabilized by two disulphide bonds, which is structurally related to allergens such as Blo t 12 that contain carbohydrate binding domains that bind chitin. Functional assays failed to confirm chitin binding by Der p 23. Conclusions and clinical relevance Der p 23 accounts for a small percentage of the IgE response to mite allergens, which is dominated by Der p 1 and Der p 2. The prevalence and amount of specific IgE to Der p 23 and Der p 2 are disproportionately high compared to the expression of other Dermatophagoides allergens. |
| Databáze: | OpenAIRE |
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