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- Title
Secret of the major birch pollen allergen Bet v 1: identification of the physiological ligand.
- Authors
SEUTTER VON LOETZEN, Christian; HOFFMANN, Thomas; HARTL, Maximilian J.; SCHWEIMER, Kristian; SCHWAB, Wilfried; RÖSCH, Paul; HARTL-SPIEGELHAUER, Olivia
- Abstract
The major birch pollen allergen Bet v 1 is the main elicitor of airborne type I allergies and belongs to the PR-10 family (pathogenesis-related proteins 10). Bet v 1 is the most extensively studied allergen, and is well characterized at a biochemical and immunological level; however, its physiological function remains elusive. In the present study, we identify Q3OS (quercetin-3-Osophoroside) as the natural ligand of Bet v 1. We isolated Q3OS bound to Bet v 1 from mature birch pollen and confirmed its binding by reconstitution of the Bet v 1-Q3OS complex. Fluorescence and UV-visible spectroscopy experiments, as well as HSQC (heteronuclear single-quantum coherence) titration, and the comparison with model compounds, such as quercetin, indicated the specificity of Q3OS binding. Elucidation of the binding site by NMR combined with a computational model resulted in a more detailed understanding and shed light on the physiological function of Bet v 1. We postulate that the binding of Q3OS to Bet v 1 plays an important, but as yet unclear, role during the inflammation response and Bet v 1 recognition by IgE.
- Subjects
HAY-fever plants; INFLAMMATION; QUERCETIN; EUROPEAN white birch; AMINO acid sequence; NUCLEAR magnetic resonance
- Publication
Biochemical Journal, 2014, Vol 457, Issue 3, p379
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BJ20130413