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Identification of a natural ligand of the hazel allergen Cor a 1

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00004663
URN to cite this document: urn:nbn:de:bvb:703-epub-4663-3

Title data

Jacob, Thessa ; Seutter von Loetzen, Christian ; Reuter, Andreas ; Lacher, Ulrike ; Schiller, Dirk ; Schobert, Rainer ; Mahler, Vera ; Vieths, Stefan ; Rösch, Paul ; Schweimer, Kristian ; Wöhrl, Birgitta M.:
Identification of a natural ligand of the hazel allergen Cor a 1.
In: Scientific Reports. Vol. 9 (18 June 2019) . - No. 8714.
ISSN 2045-2322
DOI der Verlagsversion: https://doi.org/10.1038/s41598-019-44999-2

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Abstract

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 β-sheet, two short α-helices arranged in V-shape and a long C-terminal α-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-β-D-glucopyranosyl)-β-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.

Further data

Item Type: Article in a journal
Keywords: allergens; major hazel allergen; solution structure; specific ligand
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Chair Biopolymers - Apl. Prof. Dr. Birgitta Wöhrl
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-4663-3
Date Deposited: 27 Mar 2020 10:54
Last Modified: 27 Mar 2020 10:54
URI: https://epub.uni-bayreuth.de/id/eprint/4663

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