ArticleInternational journal of molecular sciences2022
The Structural Flexibility of PR-10 Food Allergens.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- Basophil Activation Test (BAT) for Diagnosing LTP Food Allergy: Where Do We Stand Now? A Systematic Review.International journal of molecular sciences · 2025Pooled it
- Current State of Celery Allergy: Is Discovering Api g 7 a Milestone in Diagnosing Celeriac-Allergic Patients?International journal of molecular sciences · 2025Review
- Trimeric Bet v 1-specific nanobodies cause strong suppression of IgE binding.Frontiers in immunology · 2024Article
- Structural Characterization of Food Allergens by Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The Acari Hypothesis, V: deciphering allergenicity.Frontiers in allergy · 2024Article
- Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance.International journal of molecular sciences · 2023Article
- Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen.Foods (Basel, Switzerland) · 2023Article
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Review
- Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1.Foods (Basel, Switzerland) · 2022Article
- pH-dependent structural diversity of profilin allergens determines thermal stability.Frontiers in allergy · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
PR-10 proteins constitute a major cause of food allergic reactions. Birch-pollen-related food allergies are triggered by the immunologic cross-reactivity of IgE antibodies with structurally homologous PR-10 proteins that are present in birch pollen and various food sources. While the three-dimensional structures of PR-10 food allergens have been characterized in detail, only a few experimental studies have addressed the structural flexibility of these proteins. In this study, we analyze the millisecond-timescale structural flexibility of thirteen PR-10 proteins from prevalent plant food sources by NMR relaxation-dispersion spectroscopy, in a comparative manner. We show that all the allergens in this study have inherently flexible protein backbones in solution, yet the extent of the structural flexibility appears to be strikingly protein-specific (but not food-source-specific). Above-average flexibility is present in the two short helices, α1 and α2, which form a V-shaped support for the long C-terminal helix α3, and shape the internal ligand-binding cavity, which is characteristic for PR-10 proteins. An in-depth analysis of the NMR relaxation-dispersion data for the PR-10 allergen from peanut reveals the presence of at least two subglobal conformational transitions on the millisecond timescale, which may be related to the release of bound low-molecular-weight ligands from the internal cavity.
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