Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5918125 | Molecular Immunology | 2009 | 8 Pages |
Abstract
Divergent immunological properties of Amb a 1α (aa 181-396) and Amb a 1β (aa 26-180) were revealed. Amb a 1β contained important IgE epitopes, whereas Amb a 1α showed low IgE binding. When compared to natural Amb a 1, all recombinant variants possessed >100-fold reduced IgE-mediated mediator release activity. At the T-cell level recombinant and natural Amb a 1 stimulated comparable T-cell responses and the T-cell reactivity was largely directed to the C-terminal part. The results demonstrated that recombinant Amb a 1α behaves as hypoallergen with reduced IgE binding but preservation of the major T-cell reactivity. In addition, recombinant Amb a 1α can be easily purified to homogeneity in large quantity and therefore represents an ideal candidate for specific immunotherapy.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Nicole Wopfner, Beatrice Jahn-Schmid, Georg Schmidt, Tanja Christ, Gudrun Hubinger, Peter Briza, Christian Radauer, Barbara Bohle, Lothar Vogel, Christof Ebner, Riccardo Asero, Fatima Ferreira, Robert Schwarzenbacher,