[HTML][HTML] Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen

Y Machado, R Freier, S Scheiblhofer… - Journal of Allergy and …, 2016 - Elsevier
Background The search for intrinsic factors, which account for a protein's capability to act as
an allergen, is ongoing. Fold stability has been identified as a molecular feature that affects …

Naturally processed T cell–activating peptides of the major birch pollen allergen

S Mutschlechner, M Egger, P Briza, M Wallner… - Journal of allergy and …, 2010 - Elsevier
BACKGROUND: Although antigen processing and presentation of allergens to CD4+ T
lymphocytes are key events in the pathophysiology of allergic disorders, they still remain …

[HTML][HTML] Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties

S Kofler, C Ackaert, M Samonig, C Asam, P Briza… - Journal of Biological …, 2014 - ASBMB
Many allergens share several biophysical characteristics, including the capability to undergo
oligomerization. The dimerization mechanism in Bet v 1 and its allergenic properties are so …

[HTML][HTML] Stability of allergens

J Pekar, D Ret, E Untersmayr - Molecular immunology, 2018 - Elsevier
For proteins to cause IgE-mediated allergic reactions, several common characteristics have
to be defined, including small molecular size, solubility and stability to changing pH levels …

Multiple roles of Bet v 1 ligands in allergen stabilization and modulation of endosomal protease activity

WT Soh, L Aglas, GA Mueller, S Gilles, R Weiss… - Allergy, 2019 - Wiley Online Library
Background Over 100 million people worldwide suffer from birch pollen allergy. Bet v 1 has
been identified as the major birch pollen allergen. However, the molecular mechanisms of …

The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes

JE Mogensen, M Ferreras, R Wimmer, SV Petersen… - Biochemistry, 2007 - ACS Publications
The 159 residue Bet v 1 is the major allergen from birch tree pollen. Its natural function is
unknown although it is capable of binding several types of physiologically relevant ligands …

[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 …

[HTML][HTML] 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] The influence of recombinant production on the immunologic behavior of birch pollen isoallergens

M Wallner, M Himly, A Neubauer, A Erler, M Hauser… - PloS one, 2009 - journals.plos.org
Background Allergic reactions towards the birch major pollen allergen Bet v 1 are among the
most common causes of spring pollinosis in the temperate climate zone of the Northern …

Elimination of a misfolded folding intermediate by a single point mutation

JE Mogensen, H Ipsen, J Holm, DE Otzen - Biochemistry, 2004 - ACS Publications
We present an analysis of the folding behavior of the 159-residue major birch pollen
allergen Bet v 1. The protein contains a water-filled channel running through it …