Structural and epitope characterization of dust mites allergens, Der f 13 and Blo t 5

Abstract

The structure of Der f 13, a group 13 allergen from dust mite Dermatophagoides farinae was solved using NMR spectroscopy. Epitope residues have been identified and mapped to Glu-41, Lys-63, Lys-91 and Lys-103. A triple mutant 3A (E41A_K63A_K91A) has been generated and shown to stimulate the release of Th1 cytokines in patientsa?? PBMC while at the same time reducing the secretion of Th2 cytokines. The 3A mutant is able to stimulate mouse IgG antibodies that are able to inhibit the binding of patientsa?? IgE to wild type Der f 13, indicating its potential as candidate for vaccine immunotherapy against Der f 13 allergy. Structural characterization of Blo t 5, from Blomia tropicalis has also been carried out using CD and NMR spectroscopy. Backbone chemical shifts of Blo t 5 have also been assigned and three I?- helices separated by tight turns were observed in the chemical shift index plot.