The aim of our research is gaining a deeper understanding of the molecular basis and the clinical relevance of allergen-specific antibody responses. In accordance with the group's name, we employ a synergistic approach combining wet-lab experiments and in silico analyses to contribute to the progress in diagnosis and treatment of allergy.
Christian Radauer
Phone: +43 1 40400 51030
E-mail: christian.radauer (at) meduniwien.ac.at
ORCID: 0000-0001-9920-4449
Publicationen at PubMed
Christian Radauer studied Biochemistry at the University of Vienna. He performed his PhD studies in the group of Heimo Breiteneder at the former Department of General and Experimental Pathology of the University of Vienna (which is now the Department of Pathophysiology and Allergy Research of the Medical University of Vienna). Christian received his PhD degree in 2000. He continued his career in Heimo Breiteneder's lab as a post-doctoral scientist. During a short research stay in Peter Lackner's group at the Department of Molecular Biology, University of Salzburg, he gained additional experience in bioinformatics. In 2009, he received the teaching qualification (Habilitation) in molecular allergology.
Christian Radauer's research interests have focused on the field of molecular allergology. The main topics are elucidating molecular properties of allergies, factors that make certain proteins allergenic, the molecular basis of cross-reactivity, and the clinical relevance of patient specific repertoires of allergen specific immunoglobulins. Since April 2022, Christian Radauer has been scientific co-chair of the WHO/IUIS Allergen Nomenclature Sub-Committee. This function of this committee is to develop an official, unambiguous nomenclature for allergenic proteins and to make the official allergen names accessible to the scientific community in the WHO/IUIS Allergen Nomenclature Database.
Petra Natascha Hendler
Administrative assistant
Division of Medical Biotechnology
Phone: +43 1 40400 51120
E-mail: petra-natascha.hendler@meduniwien.ac.at
Nadine Prammer
Laboratory technician
Phone: +43 1 40400 51160
E-mail: nadine.prammer@meduniwien.ac.at
Clinical relevance of epitope recognition patterns of allergen-specific IgE antibodies
Many forms of respiratory allergy are associated with food allergy. 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, celery and many more. This cross-reaction is caused by IgE antibodies that recognize not only the major birch pollen allergen, Bet v 1, but also related allergens in plant foods. 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 having IgE antibodies to Bet v 1.
We hypothesize that the varying clinical relevance of IgE reactivity to Bet v 1-related food allergens may be a consequence of patient-specific IgE binding patterns to different sites (epitopes) on the surface of Bet v 1. The aim of this project is the identification of these epitopes and the elucidation of their importance for birch pollen associated food allergy. To this end, we transferred surface patches of Bet v 1 onto the surface of a non-IgE binding structural Bet v 1 homologue. These proteins, each carrying a single potential epitope, were tested for binding of IgE from birch pollen allergic patients. We are currently working on obtaining a representative overview of the epitope recognition patterns of Bet v 1-specific IgE in a large group of birch pollen-allergic patients with different profiles of food allergies. Results of the project will enable the development of epitope-based diagnostic reagents that may allow clinicians to give birch pollen allergic patients more precise dietary advice.
Selected publications
- Schmalz S, Mayr V, Shosherova A, Gepp B, Ackerbauer D, Sturm G, Bohle B, Breiteneder H, Radauer C (2022): Isotype-specific binding patterns of serum antibodies to multiple conformational epitopes of Bet v 1. J Allergy Clin Immunol 149: 1786-94. [Free full text]
- Tscheppe A, Palmberger D, van Rijt L, Kalic T, Mayr V, Palladino C, Kitzmüller C, Hemmer W, Hafner C, Bublin M, van Ree R, Grabherr R, Radauer C, Breiteneder H (2020): Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity. J Allergy Clin Immunol 145: 229-38. [Free full text]
Can the comparison of allergen sequences help us in understanding the allergenic properties of proteins?
One of the unresolved problems in allergy research is the question what makes a protein allergenic. Besides examining the behaviour of immune cells or model animals upon contact with allergenic and non-allergenic proteins, the availability of large allergen databases in combination with sequence, structure and protein family data now enables researchers to use sequence and structural analysis to gain new insights that inspire novel experimental approaches.
We aim at answering some of the following questions. What is the distribution of allergenic and non-allergenic proteins within allergen-containing protein families and superfamilies? Which sequence-related factors, such as similarity to human homologues, similarity to parasite or bacterial proteins or sequence conservation within a protein family, show a connection to allergenicity? How reliably can IgE cross-reactivity between homologous allergens be predicted based on sequence similarity data?
Selected publications
- Radauer C, Lackner P, Breiteneder H (2008): The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol Biol 8: 286. [Free full text]
Development and maintenance of the AllFam database
Most allergenic proteins can be classified into an astonishingly small number of families. Members of these protein families possess similar structures and, in many cases, similar biochemical functions. This led to the hypothesis that allergenicity depends on structural or functional characteristics of proteins. In addition, common protein family membership is a prerequisite of IgE and T cell cross-reactivity.
In order to help researchers and clinicians getting an overview of families of allergens and their allergenic members, we developed the AllFam allergen family database, a Web resource that enables the user to get protein family data for allergens compiled from the WHO/IUIS Allergen Nomenclature Database and AllergenOnline.
Selected publications
Radauer C, Breiteneder H (2019): Allergen databases - A critical evaluation. Allergy 74: 2057-2060. [Free full text]
Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H (2008): Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol 121: 847-52. [Full text]