Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1
Kofler, S., Asam, C., Eckhard, U., Wallner, M., Ferreira, F, and Brandsetter, H.

Abstract
The birch pollen contains several closely related Bet v 1 proteins isoforms. While the hyperallergenic isoforms are responsible for birch pollen allergies, there are closely related isoforms with starkly different immunologic properties, referred to as hypo-allergenic isoforms. While mechanistically poorly understood, the allergenic properties of these proteins are thought to be related to their ligand binding properties. In the awarded publication Stefan Kofler and colleagues determined high-resolution crystal structures of Bet v 1 in complex with several ligands. Unexpectedly, variations in residue 30 induce a drastic change in ligand binding. These variations correlate with the allergenicity of the respective Bet v 1 isoforms. The structural analysis further reveals key interaction residues like Tyr83, thus rationalizing the binding promiscuity of the hydrophobic pocket in Bet v 1.

The open access article can be found  here.

Reviewed by Gerhard Obermeyer