6r3c

Publication Abstract from PubMed

Hazelnut is one of the most frequent causes of food allergy. The major hazel allergen in Northern Europe is Cor a 1, which is homologous to the major birch pollen allergen Bet v 1. Both allergens belong to the pathogenesis related class PR-10. We determined the solution structure of Cor a 1.0401 from hazelnut and identified a natural ligand of the protein. The structure reveals the protein fold characteristic for PR-10 family members, which consists of a seven-stranded antiparallel beta-sheet, two short alpha-helices arranged in V-shape and a long C-terminal alpha-helix encompassing a hydrophobic pocket. However, despite the structural similarities between Cor a 1 and Bet v 1, they bind different ligands. We have shown previously that Bet v 1 binds to quercetin-3-O-sophoroside. Here, we isolated Cor a 1 from hazel pollen and identified the bound ligand, quercetin-3-O-(2"-O-beta-D-glucopyranosyl)-beta-D-galactopyranoside, by mass spectrometry and nuclear magnetic resonance spectroscopy (NMR). NMR experiments were performed to confirm binding. Remarkably, although it has been shown that PR-10 allergens show promiscuous binding behaviour in vitro, we can demonstrate that Cor a 1.0401 and Bet v 1.0101 exhibit highly selective binding for their specific ligand but not for the respective ligand of the other allergen.

Identification of a natural ligand of the hazel allergen Cor a 1.,Jacob T, von Loetzen CS, Reuter A, Lacher U, Schiller D, Schobert R, Mahler V, Vieths S, Rosch P, Schweimer K, Wohrl BM Sci Rep. 2019 Jun 18;9(1):8714. doi: 10.1038/s41598-019-44999-2. PMID:31213622^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.