| Literature DB >> 24171862 |
Christian Seutter von Loetzen1, Thomas Hoffmann2, Maximilian J Hartl1, Kristian Schweimer1, Wilfried Schwab2, Paul Rösch1, Olivia Hartl-Spiegelhauer1.
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-O-sophoroside) 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.Entities:
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Year: 2014 PMID: 24171862 DOI: 10.1042/BJ20130413
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857