Conformational flexibility differentiates naturally occurring Bet v 1 isoforms

S Grutsch, JE Fuchs, L Ahammer, AS Kamenik… - International Journal of …, 2017 - mdpi.com
The protein Bet v 1 represents the main cause for allergic reactions to birch pollen in Europe
and North America. Structurally homologous isoforms of Bet v 1 can have different properties …

Two distinct conformations in Bet v 2 determine its proteolytic resistance to cathepsin S

WT Soh, P Briza, E Dall, C Asam, M Schubert… - International journal of …, 2017 - mdpi.com
Birch pollen allergy affects more than 20% of the European allergic population. On a
molecular level, birch pollen allergy can be linked to the two dominant allergens Bet v 1 and …

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

L Ahammer, S Grutsch, M Wallner, F Ferreira… - Biomolecular NMR …, 2017 - Springer
Abstract In Northern America and Europe a great number of people are suffering from birch
pollen allergy and pollen related food allergies. The trigger for these immunological …

Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity

R Freier, E Dall, H Brandstetter - Scientific reports, 2015 - nature.com
Despite a high similarity with homologous protein families, only few proteins trigger an
allergic immune response with characteristic TH2 polarization. This puzzling observation is …

[HTML][HTML] Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen bet v 1

S Kofler, C Asam, U Eckhard, M Wallner… - Journal of molecular …, 2012 - Elsevier
The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands
is considered to play a key role for their physiological and pathological functions. In …

Expression in Escherichia coli, Purification, and Spectroscopic Characterization of Two Mutant Bet v 1 Proteins

M Boehm, P Rösch - Biological Chemistry, 1997 - degruyter.com
Bet v 1 is the major birch pollen allergen. A highly efficient expression and purification
scheme for mutant forms of this protein was developed on the basis of the pET expression …

Dynamics rationalize proteolytic susceptibility of the major birch pollen allergen Bet v 1

AS Kamenik, F Hofer, PH Handle… - Frontiers in Molecular …, 2020 - frontiersin.org
Proteolytic susceptibility during endolysosomal degradation is decisive for allergic
sensitization. In the major birch pollen allergen Bet v 1 most protease cleavage sites are …

Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen

S Grutsch, JE Fuchs, R Freier, S Kofler, M Bibi… - Biophysical …, 2014 - cell.com
Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and
transport of small molecules. A prominent member of the PR-10 family, the major birch …

[HTML][HTML] Structural study of biologically significant ligands with major birch pollen allergen Betv1 by docking and molecular dynamics simulation

S Kundu, D Roy - Bioinformation, 2010 - ncbi.nlm.nih.gov
The major birch pollen allergen, Betv1 of Betula verrucosa is the main causative agent of
birch pollen allergy in humans. Betv1 is capable of binding several physiological ligands …

Crystallization and preliminary x‐ray investigation at 2.0 Å resolution of Bet v 1, a birch pollen protein causing IgE‐mediated allergy

MD Spangfort, JN Larsen… - … : Structure, Function, and …, 1996 - Wiley Online Library
The 17 kDa protein from Betula verrucosa (White Birch) pollen, Bet v 1, is the clinically most
important birch pollen allergen causing immediate Type I IgE‐mediated allergy. The three …