ArticleProceedings of the National Academy of Sciences of the United States of America2019
Designer covalent heterobivalent inhibitors prevent IgE-dependent responses to peanut allergen.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Design of allergen-specific inhibitors against shrimp-induced allergic response.The journal of allergy and clinical immunology. Global · 2026Article
- Whence and wherefore IgE?Immunological reviews · 2024Review
- Self-Assembling Allergen Vaccine Platform Raises Therapeutic Allergen-Specific IgG Responses without Induction of Systemic Allergic Responses.ACS biomaterials science & engineering · 2024Article
- Peanut allergen inhibition prevents anaphylaxis in a humanized mouse model.Science translational medicine · 2023Article
- Determination of immunogenic epitopes in major house dust mite allergen, Der p 2, via nanoallergens.Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology · 2022Article
- Nanoarchitectures for efficient IgE cross-linking on effector cells to study amoxicillin allergy.Allergy · 2021Article
- The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds.The Journal of allergy and clinical immunology · 2021Review
- Novel Approaches in the Inhibition of IgE-Induced Mast Cell Reactivity in Food Allergy.Frontiers in immunology · 2021Review
- The design and development of covalent protein-protein interaction inhibitors for cancer treatment.Journal of hematology & oncology · 2020Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Allergies are a result of allergen proteins cross-linking allergen-specific IgE (sIgE) on the surface of mast cells and basophils. The diversity and complexity of allergen epitopes, and high-affinity of the sIgE-allergen interaction have impaired the development of allergen-specific inhibitors of allergic responses. This study presents a design of food allergen-specific sIgE inhibitors named covalent heterobivalent inhibitors (cHBIs) that selectively form covalent bonds to only sIgEs, thereby permanently inhibiting them. Using screening reagents termed nanoallergens, we identified two immunodominant epitopes in peanuts that were common in a population of 16 allergic patients. Two cHBIs designed to inhibit only these two epitopes completely abrogated the allergic response in 14 of the 16 patients in an in vitro assay and inhibited basophil activation in an allergic patient ex vivo analysis. The efficacy of the cHBI design has valuable clinical implications for many allergen-specific responses and more broadly for any antibody-based disease.
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Registered trials
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