title: Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.
abstract: Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens.
authors.affiliation: Institute of Organic Chemistry, University of Innsbruck, Innsbruck, Austria.
authors.forename: Sarina
authors.initials: S
authors.lastname: Grutsch
authors.affiliation: Institute of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck, University of Innsbruck, Innsbruck, Austria.
authors.forename: Julian E
authors.initials: JE
authors.lastname: Fuchs
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Regina
authors.initials: R
authors.lastname: Freier
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Stefan
authors.initials: S
authors.lastname: Kofler
authors.affiliation: Institute of Organic Chemistry, University of Innsbruck, Innsbruck, Austria.
authors.forename: Marium
authors.initials: M
authors.lastname: Bibi
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Claudia
authors.initials: C
authors.lastname: Asam
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Michael
authors.initials: M
authors.lastname: Wallner
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Fátima
authors.initials: F
authors.lastname: Ferreira
authors.affiliation: Department of Molecular Biology, University of Salzburg, Salzburg, Austria.
authors.forename: Hans
authors.initials: H
authors.lastname: Brandstetter
authors.affiliation: Institute of General, Inorganic and Theoretical Chemistry, Center for Molecular Biosciences Innsbruck, University of Innsbruck, Innsbruck, Austria.
authors.forename: Klaus R
authors.initials: KR
authors.lastname: Liedl
authors.affiliation: Institute of Organic Chemistry, University of Innsbruck, Innsbruck, Austria. Electronic address: martin.tollinger@uibk.ac.at.
authors.forename: Martin
authors.initials: M
authors.lastname: Tollinger
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D000595:Amino Acid Sequence; D029662:Betula / Q000737:chemistry* / Q000276:immunology; D008024:Ligands; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D011058:Pollen / Q000737:chemistry* / Q000276:immunology; D017434:Protein Structure, Tertiary
chemical_list: D000485:Allergens; D008024:Ligands; D010940:Plant Proteins