Food Allergens

Allergens with very similar structures can display drastically different immunologic properties. We are investigating whether and to what extent the intrinsic structural flexibility of allergenic proteins is immunologically relevant. Local flexibility could be in­volved in antibody rbinding and re­present a mechanism for the proteo­lytic processing of allergenic proteins via the transient exposure of pro­teolytic cleavage sites to the protein surface. In recent publications we have determined three-dimensional structures and flexibilities of cross-allergenic PR-10 allergens from apple and birch pollen.

Collaboration with

Laimburg Research Centre for Agriculture and Forestry   

Klaus R. Liedl (University of Innsbruck)   

Christian Radauer (Medical University of Vienna)   

Richard Weiss (University of Salzburg)   


Recent publications (allergens)


Führer S, Trimmel S,  Breuker K, Tollinger M*.

        NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101.

        Biomol NMR Assign: accepted for publication. (open access)

        doi: 10.1007/---


Grutsch S, Fuchs JE, Ahammer L, Kamenik AS, Liedl KR*, Tollinger M*.

Conformational flexibility differentiates naturally occurring Bet v 1 isoforms.

Int J Mol Sci 2017 (18) 1192. (open access)

doi: 10.3390/ijms1806119


Ahammer L, Grutsch S, Kamenik AS, Liedl KR, Tollinger M*.

Structure of the major apple allergen Mal d 1.

J Agricult Food Chem 2017 (65): 1606-1612. (open access)

doi: 10.1021/acs.jafc.6b05752


Ahammer L, Grutsch S, Wallner M, Ferreira F, Tollinger M*.

NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1.

Biomol NMR Assign 2017 (11): 231-234. (open access)

doi: 10.1007/s12104-017-9754-7


Ahammer L, Grutsch STollinger M*.

NMR resonance assignments of the major apple allergen Mal d 1.

Biomol NMR Assign 2016 (10): 287-290. (open access)

doi: 10.1007/s12104-016-9685-8


Machado Y, Freier R, Scheiblhofer S, Thalhamer T, Mayr M, Briza P, Grutsch SAhammer L, Fuchs J, Wallnöfer H, Isakovic A, Kohlbauer V, Hinterholzer A, Steiner M, Danzer M, Horejs-Hoeck J, Ferreira F, Liedl KR, Tollinger M, Lackner P, Johnson CM, Brandstetter H, Thalhamer J & Weiss R*.

Fold-stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen.

Journal of Allergy and Clinical Immunology 2016 (137): 1525-1534. (open access)

doi: 10.1016/j.jaci.2015.09.026 


Grutsch S, Fuchs JE, Freier R, Kofler S, Bibi M, Asam C, Wallner M, Ferreira F, Brandstetter H, Liedl KR, Tollinger M*.

Ligand binding modulates structural dynamics and compactness of the major birch pollen allergen Bet v 1.0101.

Biophys J 2014 (107): 2963-2972. (open access)

doi: 10.1016/j.bpj.2014.10.062