Allergens; Allergy and Immunology; Biochemistry; Pollen Allergy
Many forms of inhalant allergy are associated with food allergy due to cross-reactivity between inhalant allergens and homologous food allergens. However, IgE cross-reactivity does not always translate into clinically overt food allergy. Our research focuses on the characterization of these allergens and the cross-reactive epitopes for IgE and other isotypes. Our aim is to elucidate factors that determine the clinical outcome of cross-sensitization.
The second focus of our research is related to the question which properties determine the allergenicity of a protein. By using bioinformatics analyses, we classify allergens, non-allergenic homologues and whole proteome sequences by sequence-related and structural properties with the aim of discriminating allergens from non-allergenic proteins and improve the currently insufficient methods of allergenicity prediction. An outcome of this work has been the AllFam database of allergen families, which is freely accessible on the internet at http://www.meduniwien.ac.at/allfam/
Techniques, methods & infrastructure
In addition to standard methods in molecular biology, protein chemistry and immunochemistry, we use phage libraries to - among others - select allergen-specific recombinant antibodies. Moreover, a focus of the Biochemistry and Bioinformatics group is the application of bioinformatics methods, such as functional and evolutionary classification of proteins or homology modelling and structure comparison, on the study of allergenic proteins.
- Guhsl, E.E. et al., 2014. IgE, IgG4 and IgA specific to Bet v 1-related food allergens do not predict oral allergy syndrome. Allergy, 70(1), pp.59-66. Available at: http://dx.doi.org/10.1111/all.12534.
- Gepp, B. et al., 2014. Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE responses in patients with birch pollen allergy. Journal of Allergy and Clinical Immunology, 134(1), pp.188-194. Available at: http://dx.doi.org/10.1016/j.jaci.2013.12.1073.
- Radauer, C. et al., 2011. 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. Molecular Immunology, 48(4), pp.600-609. Available at: http://dx.doi.org/10.1016/j.molimm.2010.10.019.
- Radauer, C., Lackner, P. & Breiteneder, H., 2008. The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evolutionary Biology, 8(1), p.286. Available at: http://dx.doi.org/10.1186/1471-2148-8-286.
- Radauer, C. et al., 2008. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. Journal of Allergy and Clinical Immunology, 121(4), pp.847-852.e7. Available at: http://dx.doi.org/10.1016/j.jaci.2008.01.025.