Structural Basis for Trivalent Cross‐Linking of a Patient‐Derived <scp>IgE</scp> Antibody by the Major Peanut Allergen Ara h 2.0201

The trivalent binding is effective in forming large allergen-IgE complexes on mast cell or basophil surfaces and contributes to the potency of Ara h 2 in triggering allergic reactions and highlighting its role in anaphylaxis. Proline hydroxylation considerably enhances D08 binding affinity and contributes to cross-reactivity among Ara h 1-3 allergens.

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Publication Details

Journal
Allergy
Published
2026-02-17
DOI
https://doi.org/10.1111/all.70258
Primary Topic
Food Allergy and Anaphylaxis Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural Basis for Trivalent Cross‐Linking of a Patient‐Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201

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article

Structural Basis for Trivalent Cross‐Linking of a Patient‐Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201

Tarja Parkkinen, Juha Rouvinen, Janne Jänis, Heidi Heiniluoto, Kristiina Takkinen
article en

Abstract

The trivalent binding is effective in forming large allergen-IgE complexes on mast cell or basophil surfaces and contributes to the potency of Ara h 2 in triggering allergic reactions and highlighting its role in anaphylaxis. Proline hydroxylation considerably enhances D08 binding affinity and contributes to cross-reactivity among Ara h 1-3 allergens.

Allergy
University of Eastern Finland (FI), Fortum (Finland) (FI)
Itä-Suomen Yliopisto, Biocenter Finland
Zero hunger
Openalex Percentile: Top 44%
Food Allergy and Anaphylaxis Research
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