Detail

Keywords

Allergens; Allergy and Immunology; Biochemistry; Pollen Allergy

Research group(s)

• Biochemistry and Bioinformatics
  Head: Christian Radauer
  Research Area: Gaining a deeper understanding of the molecular basis and the clinical relevance of the allergen-specific humoral immune response as well as elucidating molecular properties of allergenic proteins that contribute to their allergenicity.
  Members:
  Christian Radauer

Research interests

One factor proposed to determine the clinical outcome of allergic sensitization are the epitope binding patterns of allergen-specific IgE and IgG. To identify conformational epitopes, we have developed an approach based on chimeric proteins that carry distinct patches derived from the allergen surface. We are applying this approach to characterizing epitope binding patterns of antibodies from patients allergic to birch and grass pollen. In birch pollen allergy, we want to understand why patients show different patterns of allergic reactions to certain plant foods, although IgE of most patients binds to the major birch pollen allergen, Bet v 1, and cross-reacts with related allergens in those plants. In grass pollen allergy, we aim at monitoring the development of epitope recognition patterns of allergen-specific IgE and IgG during allergen immunotherapy.

Another 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 proteomes by sequence-related and structural properties with the aim of improving 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 https://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.

Grants

• Epitope recognition patterns in grass pollen allergy (2024)
  Source of Funding: FWF (Austrian Science Fund), Principal Investigator Project
  Principal Investigator
• Epitope recognition patterns of Bet v 1-specific IgE (2017)
  Source of Funding: FWF (Austrian Science Fund), Principal Investigator Project
  Principal Investigator

Selected publications

1. Schmalz, S. et al. (2022) ‘Isotype-specific binding patterns of serum antibodies to multiple conformational epitopes of Bet v 1’, Journal of Allergy and Clinical Immunology, 149(5), pp. 1786-1794.e12. Available at: http://dx.doi.org/10.1016/j.jaci.2021.10.026.
2. Tscheppe, A. et al. (2020) ‘Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity’, Journal of Allergy and Clinical Immunology, 145(1), pp. 229–238. Available at: http://dx.doi.org/10.1016/j.jaci.2019.08.036.
3. 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.
4. 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.
5. 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.