ArticleThe Journal of allergy and clinical immunology2025
Structural determinants of peanut-induced anaphylaxis.
Article in The Journal of allergy and clinical immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Immunization with Virus-Like Particles Displaying Ara h 2‑Derived Peptides to Mitigate Peanut Allergy.ACS nano medicine · 2026Article
- Structural Basis for Trivalent Cross-Linking of a Patient-Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201.Allergy · 2026Article
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- Alpha-gal-specific human IgE promotes both alpha-gal-induced and antigen-independent allergic effector cell activation.The Journal of allergy and clinical immunology · 2026Article
- Baking results in impaired detection of clinically relevant food allergens.Frontiers in allergy · 2026Article
- Epitope-Specific Antibodies in Allergic Disease and Clinical Tolerance.Immunological reviews · 2025Review
- Emerging diagnostic and therapeutic opportunities in food allergy.Frontiers in immunology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
backgroundHuman IgE mAbs recognizing peanut allergens have recently become available, but we lack a detailed understanding of how these IgEs target allergens.
objectiveWe sought to determine the molecular details of the antibody-allergen interaction for a panel of clinically important human IgE mAbs and to develop strategies to disrupt disease causing antibody-allergen interactions.
methodsWe identified candidates from a panel of epitope binned human IgE mAbs that recognize 2 important and homologous peanut allergens, Ara h 2 and Ara h 6. Crystal structures were determined revealing the interfaces (antigenic sites) of exemplars of 5 common IgE bins.
resultsAmong the common antigenic sites on Ara h 2 and Ara h 6, 2 sites (A and B) are highly conserved between the allergens, explaining the cross-reactivity of antibodies that recognize these sites. Three sites (C, D, and F) involve residues that are not conserved between the allergens. Of the 5 common sites, 3 sites (B, C, and D) involve residues that are near each other only when the allergens are properly folded, such that these sites are conformational. Two additional sites (sites A and F) involve largely linear stretches of amino acids. Site F targeted antibody, 38B7, binds to a peptide sequence DPYSP
conclusionWe created a structural map of the IgE antibody response to the most important peanut allergen proteins to enable the design of new allergy immunotherapies and vaccines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.