0000000001254534

AUTHOR

Elke Völker

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Quality and potency profile of eight recombinant isoallergens, largely mimicking total Bet v 1-specific IgE binding of birch pollen.

2019

Background To date, only limited information on structure, expression levels and IgE binding of Bet v 1 variants, which are simultaneously expressed in birch pollen, is available. Objective To analyse and compare structure and serum IgE/IgG binding of rBet v 1 variants to Bet v 1.0101. Methods Recombinant Bet v 1 variants were studied with sera of 20 subjects allergic to birch pollen. Folding, aggregation and solubility of the rBet v 1 variants were analysed to attribute diverging IgE binding to either allergen structure or methodological features. IgE/IgG binding was studied with rBet v 1 in solution or adsorbed to solid phases. Allergen-mediated cross-linking of FceRI receptors was determ…

MaleImmunologyEnzyme-Linked Immunosorbent AssayBasophilImmunoglobulin Emedicine.disease_causeMass Spectrometrylaw.inventionAllergenlawmedicineImmunology and AllergyPotencyAnimalsHumansReceptorBetulaPlant ProteinsbiologyChemistrySpectrum AnalysisRhinitis Allergic SeasonalHypoallergenicAntigens PlantImmunoglobulin EMolecular biologyRecombinant ProteinsRatsmedicine.anatomical_structureIgG bindingImmunoglobulin Gbiology.proteinRecombinant DNAPollenFemaleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology
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