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Purification and IgE binding capacity of Der s 3, a major allergen from Dermatophagoides siboney
Author(s) -
FERRÁNDIZ R.,
CASAS R.,
DREBORG S.
Publication year - 1997
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1997.tb01199.x
Subject(s) - allergen , polyclonal antibodies , immunoglobulin e , affinity chromatography , house dust mite , mite , antibody , chemistry , pyroglyphidae , sensitization , radioallergosorbent test , immunology , monoclonal antibody , allergy , biology , biochemistry , enzyme , botany
Summary Background Sensitization to the house dust mite Dermatophagoides siboney has been demonstrated in asthmatic patients. Previously, Dermatophagoides siboney group 1 and group 2 allergens, named Der s 1 and Der s 2, respeetively, have been purified. Objectives The aim of this study was to purify and to study the IgE reactivity of a 30 kDa component, suspected to correspond to group 3 allergens. Methods The protein was purified by affinity chromatography using anti‐Der f 3 monoclonal antibodies and semi‐preparative SDS‐PAGE. The IgE binding capacity of the purified fractions was tested with sera from 106 mite‐ sensitive asthmatic patients using a modified chemiluminiscent method. Results Affinity chromatography resulted in fractions containing the 30 kDa component which was further purified to homogeneity by SDS‐PAGE. Seventythree per cent of the sera showed IgE reactivity to this protein, indicating that it is a major allergen. The protein also reacted with anti Der f 3 polyclonal antibodies and had tryptic activity. There were differences in the reaetivity to Der s 3 according to the age of the patients. Conclusion Based on the frequency of IgE reactions and the reactivity with antibodies directed to Der f 3, it is proposed to name this 30 kDa allergen from D. siboney , Der s 3.