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Purification and IgE binding capacity of Der s 3, a major allergen from Dermatophagoides siboney
R Ferrándiz1, R Casas, S Dreborg
1Department of Paediatrics, Linköping University Hospital, Sweden.
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, respectively, have been purified.
Objectives:
The aim of this study was to purify and to study the IgE reactivity of 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. Seventy-three 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 reactivity 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.