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Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.

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Führer S, Kamenik AS, Zeindl R, Nothegger B, Hofer F, Reider N, Liedl KR, Tollinger M
OpenAccess logo Sci Rep 11 4173 (2021)
Related entries: 6y3h, 6y3k, 6y3l

Cited: 11 times
EuropePMC logo PMID: 33603065

Abstract

A major proportion of allergic reactions to hazelnuts (Corylus avellana) are caused by immunologic cross-reactivity of IgE antibodies to pathogenesis-related class 10 (PR-10) proteins. Intriguingly, the four known isoforms of the hazelnut PR-10 allergen Cor a 1, denoted as Cor a 1.0401-Cor a 1.0404, share sequence identities exceeding 97% but possess different immunologic properties. In this work we describe the NMR solution structures of these proteins and provide an in-depth study of their biophysical properties. Despite sharing highly similar three-dimensional structures, the four isoforms exhibit remarkable differences regarding structural flexibility, hydrogen bonding and thermal stability. Our experimental data reveal an inverse relation between structural flexibility and IgE-binding in ELISA experiments, with the most flexible isoform having the lowest IgE-binding potential, while the isoform with the most rigid backbone scaffold displays the highest immunologic reactivity. These results point towards a significant entropic contribution to the process of antibody binding.

Articles - 6y3i mentioned but not cited (3)

  1. Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens. Führer S, Kamenik AS, Zeindl R, Nothegger B, Hofer F, Reider N, Liedl KR, Tollinger M. Sci Rep 11 4173 (2021)
  2. The Structural Flexibility of PR-10 Food Allergens. Führer S, Unterhauser J, Zeindl R, Eidelpes R, Fernández-Quintero ML, Liedl KR, Tollinger M. Int J Mol Sci 23 8252 (2022)
  3. The updated Structural Database of Allergenic Proteins (SDAP 2.0) provides 3D models for allergens and incorporated bioinformatics tools. Negi SS, Schein CH, Braun W. J Allergy Clin Immunol Glob 2 100162 (2023)


Reviews citing this publication (1)

  1. A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance. Sharma E, Vitte J. J Allergy Clin Immunol Glob 3 100230 (2024)

Articles citing this publication (7)

  1. Structure and Zeatin Binding of the Peach Allergen Pru p 1. Eidelpes R, Hofer F, Röck M, Führer S, Kamenik AS, Liedl KR, Tollinger M. J Agric Food Chem 69 8120-8129 (2021)
  2. Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1. Chebib S, Schwab W. Foods 10 2771 (2021)
  3. Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1. Ahammer L, Unterhauser J, Eidelpes R, Meisenbichler C, Nothegger B, Covaciu CE, Cova V, Kamenik AS, Liedl KR, Breuker K, Eisendle K, Reider N, Letschka T, Tollinger M. Foods 11 2953 (2022)
  4. Structural Characterization of Food Allergens by Nuclear Magnetic Resonance Spectroscopy. Zeindl R, Unterhauser J, Röck M, Eidelpes R, Führer S, Tollinger M. Methods Mol Biol 2717 159-173 (2024)
  5. Allergenicity and structural properties of new Cor a 1 isoallergens from hazel identified in different plant tissues. Hendrich JM, Reuter A, Jacob TP, Kara H, Amer S, Rödel K, Wöhrl BM. Sci Rep 14 5618 (2024)
  6. Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen. Zeindl R, Franzmann AL, Fernández-Quintero ML, Seidler CA, Hoerschinger VJ, Liedl KR, Tollinger M. Foods 12 3939 (2023)
  7. The role of the DE and EF loop of BKPyV VP1 in the serological cross-reactivity between subtypes. Hejtmánková A, Caisová H, Tomanová T, Španielová H. Virus Res 324 199031 (2023)


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