Freier, Regina: Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity. . In: Scientific Reports. Jg.5, S.19
- Early Bet v 1 cleavage sites are not accessible to proteases.
- Figure 1. Bet v 1 cleavage sites are cryptic and require reordering for protease access.
- Binding of Bet v 1 isoforms to immobilized cathepsin S revealed low affinity sites in Bet v 1a, but high affinity sites in ...
- Figure 2. Binding affinity of cathepsin S is four times higher towards Bet v 1d than Bet v 1a.
- Differences in the fold flexibility of Bet v 1 isoforms relate to their different affinities towards cathepsin S.
- Figure 3. Degradation of Bet v 1a by active wild type cathepsin S was significantly slower as compared to more rapidly digested Bet v 1d.
- Figure 4. Convergence of binding affinities upon structural destabilization.
- Figure 5. Binding to cathepsin S is pH-dependent and differs significantly between Bet v 1 isoforms.
- Figure 6. pH-dependent proteolytic resistance of Bet v 1a and 1d selects for the protein degradation and antigen presentation pathway, respectively.
- Cloning, expression, and purification of cathepsin S.
- Expression and purification of Bet v 1a and 1d.
- Proteolytic processing assay.
- Interaction studies using SAW-technology (Surface Acoustic Waves).
- Induction and control of destabilized Bet v 1.
- Author Contributions