ArticleJournal of molecular biology2012
Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen bet v 1.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Bet v 1 from birch pollen is a lipocalin-like protein acting as allergen only when devoid of iron by promoting Th2 lymphocytes.The Journal of biological chemistry · 2014Trial
- Article
- Identification of glycosylated flavonoids as new physiological ligands of the hazel allergen Cor a 1: Complex structures reveal different binding orientation and specificity of mono- and disaccharide derivatives.Food chemistry: X · 2025Article
- An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025Article
- Insights into structural and binding studies of pollen allergen Bet v 1 using computational approaches.In silico pharmacology · 2025Article
- Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues.Scientific reports · 2024Article
- Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?Frontiers in allergy · 2024Review
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Major latex-like proteins show pH dependency in their binding to hydrophobic organic pollutants.Journal of pesticide science · 2023Article
- The History and Science of the Major Birch Pollen Allergen Bet v 1.Biomolecules · 2023Review
- Birch pollen-The unpleasant herald of spring.Frontiers in allergy · 2023Review
- Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5.Frontiers in allergy · 2023Review
- Binding to Iron Quercetin Complexes Increases the Antioxidant Capacity of the Major Birch Pollen Allergen Bet v 1 and Reduces Its Allergenicity.Antioxidants (Basel, Switzerland) · 2022Article
- Review
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Structural Alterations of Antigens at the Material Interface: An Early Decision Toolbox Facilitating Safe-by-Design Nanovaccine Development.International journal of molecular sciences · 2021Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
- Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating binding properties of naturally occurring Bet v 1 variants, are poorly understood. Here, we report crystal structures of Bet v 1 variants in complex with an array of ligands at a resolution of up to 1.2 Å. Residue 30 within the hydrophobic pocket not only discriminates in high and low IgE binding Bet v 1 isoforms but also induces a drastic change in the binding mode of the model ligand deoxycholate. Ternary crystal structure complexes of Bet v 1 with several ligands together with the fluorogenic reporter 1-anilino-8-naphthalene sulfonate explain anomalous fluorescence binding curves obtained from 1-anilino-8-naphthalene sulfonate displacement assays. The structures reveal key interaction residues such as Tyr83 and rationalize both the binding specificity and promiscuity of the so-called hydrophobic pocket in Bet v 1. The intermolecular interactions of Bet v 1 reveal an unexpected complexity that will be indispensable to fully understand its roles within the physiological and allergenic context.
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