ArticleInternational journal of molecular sciences2017
Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Structural Characterization of Food Allergens by Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- To stay or not to stay intact as an allergen: the endolysosomal degradation assay used as tool to analyze protein immunogenicity andFrontiers in allergy · 2024Review
- Spatiotemporal proteolytic susceptibility of allergens: positive or negative effects on the allergic sensitization?Frontiers in allergy · 2024Review
- Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen.Foods (Basel, Switzerland) · 2023Article
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Bet v 1 and other birch allergens are more resistant to proteolysis and more abundant than other birch pollen proteins.Allergy · 2022Article
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
- Abundance and Stability as Common Properties of Allergens.Frontiers in allergy · 2021Review
- Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family.Current allergy and asthma reports · 2020Review
- Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1.Frontiers in molecular biosciences · 2020Article
- pH-Induced Local Unfolding of the Phl p 6 Pollen Allergen From cpH-MD.Frontiers in molecular biosciences · 2020Article
- Hydrophobic ligands influence the structure, stability, and processing of the major cockroach allergen Bla g 1.Scientific reports · 2019Article
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Authors and funding
6 authors.
Funding
Abstract
The protein Bet v 1 represents the main cause for allergic reactions to birch pollen in Europe and North America. Structurally homologous isoforms of Bet v 1 can have different properties regarding allergic sensitization and Th2 polarization, most likely due to differential susceptibility to proteolytic cleavage. Using NMR relaxation experiments and molecular dynamics simulations, we demonstrate that the initial proteolytic cleavage sites in two naturally occurring Bet v 1 isoforms, Bet v 1.0101 (Bet v 1a) and Bet v 1.0102 (Bet v 1d), are conformationally flexible. Inaccessible cleavage sites in helices and strands are highly flexible on the microsecond-millisecond time scale, whereas those located in loops display faster nanosecond-microsecond flexibility. The data consistently show that Bet v 1.0102 is more flexible and conformationally heterogeneous than Bet v 1.0101. Moreover, NMR hydrogen-deuterium exchange measurements reveal that the backbone amides in Bet v 1.0102 are significantly more solvent exposed, in agreement with this isoform's higher susceptibility to proteolytic cleavage. The differential conformational flexibility of Bet v 1 isoforms, along with the transient exposure of inaccessible sites to the protein surface, may be linked to proteolytic susceptibility, representing a potential structure-based rationale for the observed differences in Th2 polarization and allergic sensitization.
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