The Structural Flexibility of PR-10 Food Allergens
| Autor: | Sebastian Führer, Jana Unterhauser, Ricarda Zeindl, Reiner Eidelpes, Monica L. Fernández-Quintero, Klaus R. Liedl, Martin Tollinger |
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| Rok vydání: | 2022 |
| Předmět: |
Organic Chemistry
protein flexibility conformational breathing ligand binding NMR spectroscopy relaxation dispersion General Medicine Allergens Antigens Plant Cross Reactions Catalysis Computer Science Applications Inorganic Chemistry Pollen Amino Acid Sequence Physical and Theoretical Chemistry Molecular Biology Spectroscopy Betula Food Hypersensitivity Plant Proteins |
| Zdroj: | International Journal of Molecular Sciences; Volume 23; Issue 15; Pages: 8252 |
| ISSN: | 1422-0067 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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