Proteolytic susceptibility during endolysosomal degradation is decisive for allergic
sensitization. In the major birch pollen allergen Bet v 1 most protease cleavage sites are …

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 …

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 …

Only a small fraction of environmental proteins encountered by the human immune system
consistently induce allergic sensitization. This suggests that the presence of specific …

Susceptibility to endosomal degradation is a decisive contribution to a protein's
immunogenicity. It is assumed that the processing kinetics of structured proteins are …

Despite a high similarity with homologous protein families, only few proteins trigger an
allergic immune response with characteristic TH2 polarization. This puzzling observation is …

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 …

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 …

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 …

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 …