| Autor: |
Simon-Nobbe, Birgit, Probst, Gerald, Kajava, Andrey V., Oberkofler, Hannes, Susani, Markus, Crameri, Reto, Ferreira, Fátima, Ebner, Christof, Breitenbach, Michael |
| Zdroj: |
The Journal of Allergy and Clinical Immunology; November 2000, Vol. 106 Issue: 5 p887-895, 9p |
| Abstrakt: |
Background:Cladosporium herbarumand Alternaria alternataare two of the most prominent fungal species inducing type I allergy. Previously, we have demonstrated that enolase (Cla h 6) is the second most important allergen of C herbarumin terms of frequency of sensitization. Objective:IgE-reactive B-cell epitopes of C herbarumenolase were analyzed, and cross-reactivity between fungal enolases was investigated. Methods:Cla h 6 glutathione-S-transferase fusion peptides were constructed by means of PCR cloning. A alternataenolase (Alt a 5) was isolated by screening a complementary (c)DNA expression library with a C herbarumenolase DNA probe. Results:Mapping of Cla h 6 IgE-binding epitopes identified a peptide with a length of 69 amino acids (peptide 9), which bound IgE from 8 of 8 patients. Analysis of the conformation of peptide 9 revealed that it does not form a compact structure but rather spans the whole length of the protein, with side chains exposed to solvent at 3 locations. Peptide 9 in the context of Escherichia coliglutathione-S-transferase not only binds IgE but also competitively inhibits IgE binding to Alt a 5. This result indicates that the epitope or epitopes on peptide 9 constitute a major cross-reacting epitope or epitopes on the enolases from C herbarumand A alternatain the case of the one patient tested. Conclusions:We demonstrated that the glycolytic enzyme enolase is an allergen not only in C herbarumbut also in A alternata. Additionally, enolase was shown to exhibit high cross-reactivity to other fungal enolases. On the basis of the results presented here, we propose the use of recombinant Cla h 6 or maybe even peptide 9 of Cla h 6 for diagnosis and possibly therapy of mold allergy. (J Allergy Clin Immunol 2000;106:887-95.) |
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