Purified natural and recombinant Fel d 1 and cat albumin in in vitro diagnostics for cat allergy
Autor: | Julian F. Bond, W. Astrid van Leeuwen, Ronald van Ree, Ingrid Bulder, Rob C. Aalberse |
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Přispěvatelé: | Other departments |
Jazyk: | angličtina |
Rok vydání: | 1999 |
Předmět: |
Allergy
Immunology medicine.disease_cause Immunoglobulin E law.invention Pichia pastoris Radioallergosorbent Test Allergen law immune system diseases Fel d 1 Hypersensitivity medicine otorhinolaryngologic diseases Animals Immunology and Allergy Serum Albumin Glycoproteins House dust mite biology medicine.diagnostic_test Chemistry Radioallergosorbent test Allergens biology.organism_classification medicine.disease Molecular biology Recombinant Proteins respiratory tract diseases Cats Recombinant DNA biology.protein |
Zdroj: | Journal of allergy and clinical immunology, 104(6), 1223-1230. Mosby Inc. |
ISSN: | 0091-6749 |
DOI: | 10.1016/s0091-6749(99)70017-5 |
Popis: | Background: Current diagnostics and therapeutics for cat allergy are based on cat epithelial extracts originating from highly variable source materials. This gives rise to several problems: variability of allergen composition, contamination with house dust mite allergens, and potential transfer of pathogenic agents. Objective: The aim of this study was to investigate the feasibility of replacing cat epithelial extracts with purified natural or recombinant allergens. Methods: Sera (n = 509) were selected on the basis of a positive cat RAST result and tested in a RAST for IgE reactivity to purified Fel d 1, cat albumin (CA), or both. The analysis was performed with both natural and recombinant allergens. In addition, some sera were further analyzed by means of immunoblotting. A serum pool was used for cat RAST inhibition with purified natural and recombinant allergens as inhibitors. Results: Natural and recombinant Fel d 1 caused very similar results: 94.1% and 96.1% positive test results, respectively. In general, the negative sera were low responders to cat extract. The addition of CA (16.7% positive sera) resulted in a decrease in the number of discrepencies between purified allergens and whole extract to 2.8%. Only for 2% of all sera, sensitization to cat was largely explained by IgE reactivity to CA. IgE reactivity to Fel d 1 accounts for 88% of the total IgE response to cat allergens, as was demonstrated by RAST, with Fel d 1 concentrations nearing saturation. Recombinant Fel d 1 performed equally well in the RAST analysis. Recombinant CA was succesfully expressed in the yeast Pichia pastoris , and its immune reactivity closely resembled that of its natural counterpart. Conclusion: Natural and recombinant Fel d 1 and CA are good candidates for replacing ill-defined cat dander extracts in diagnostics for cat allergy. Although CA is not essential for the vast majority of cat-sensitized patients, some subjects are selectively sensitized to this serum protein. (J Allergy Clin Immunol 1999;104:1223-30.) |
Databáze: | OpenAIRE |
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