Advertisement
Research Article Free access | 10.1172/JCI119330
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Vrtala, S. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Hirtenlehner, K. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Vangelista, L. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Pastore, A. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Eichler, H. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Sperr, W. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Valent, P. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Ebner, C. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Kraft, D. in: JCI | PubMed | Google Scholar
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Find articles by Valenta, R. in: JCI | PubMed | Google Scholar
Published April 1, 1997 - More info
A novel approach to reduce the anaphylactic activity of allergens is suggested. The strategy makes use of the presence of conformational immunoglobulin E (IgE) epitopes on one of the most common allergens. The three dimensional structure of the major birch pollen allergen, Bet v 1, was disrupted by expressing two parts of the Bet v 1 cDNA representing amino acids 1-74 and 75-160 in Escherichia coli. In contrast to the complete recombinant Bet v 1, the fragments showed almost no allergenicity and exhibited random coil conformation as analyzed by circular dichroism. Both nonanaphylactic fragments induced proliferation of human Bet v 1-specific T cell clones, indicating that they harbored all dominant T cell epitopes and therefore may be considered as a basis for the development of a safe and specific T cell immunotherapy.