Professor of Pathophysiology and Allergy Research
Division of Medical Biotechnology
Department of Pathophysiology and Allergy Research
Center for Pathophysiology, Infectiology and Immunology
Währinger Gürtel 18-20, 1090 Vienna, Austria
Phone: +43 (0)1 40400 - 51030
FAX: +43 (0)1 40400 - 51300
Molecular basis and clinical relevance of IgE cross-reactivity in the pollen-fruit and latex-fruit syndrome, Molecular classification and evolutionary biology of allergens.
Biochemistry and Bioinformatics research group
Many forms of inhalant allergy are associated with food allergy due to cross-reactivity between inhalant allergens and homologous food allergens. For instance, about 70% of birch pollen allergic patients show adverse reactions to fruits, nuts and vegetables such as apple, hazelnut, kiwi fruit, stone fruits, celeriac and many more. However, most patients react to only a limited number of these foods and some patients even do not show any symptoms of food allergy despite being sensitized to the cross-reactive major birch pollen allergen, Bet v 1.
The hypothesis underlying our ongoing project is that the epitope recognition profile of Bet v 1-specific IgE determines the clinical consequences of Bet v 1 sensitization. Thus, we aim to identify IgE epitopes of Bet v 1 and its homologues from plant foods. To this end, artificial proteins carrying single conformational IgE epitopes on a non-IgE-binding scaffold will be generated by employing an innovative in vitro directed evolution approach. These single-epitope carriers will be used to compare IgE binding profiles with clinical symptoms in a large sample of well-characterized birch pollen allergic patients.
Basic molecular biology techniques (PCR, cloning); protein expression and purification; phage display; immunoassays (e.g. ELISA, basophil activation); physico-chemical characterization of proteins (e.g. circular dichroism spectroscopy, mass specrometry); surface plasmon resonance.
Radauer C, Adhami F, Fürtler I, Wagner S, Allwardt D, Scala E, Ebner C, Hafner C, Hemmer W, Mari A, Breiteneder H. Latex-allergic patients sensitized to the major allergen hevein and hevein-like domains of class I chitinases show no increased frequency of latex-associated plant food allergy. Mol Immunol. 2011; 48: 600-9.
Radauer C, Lackner P, Breiteneder H. The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol Biol. 2008; 8: 286.
Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol. 2008; 121: 847-52.