ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2012
An unfolded variant of the major peanut allergen Ara h 2 with decreased anaphylactic potential.
Article in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity.The Journal of allergy and clinical immunology · 2020Trial
- Alanine Scanning of the Unstructured Region of Ara h 2 and of a Related Mimotope Reveals Critical Amino Acids for IgE Binding.Molecular nutrition & food research · 2023Article
- Immunodominant conformational and linear IgE epitopes lie in a single segment of Ara h 2.The Journal of allergy and clinical immunology · 2022Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family.Foods (Basel, Switzerland) · 2021Article
- Immunotherapy of Food Allergy: a Comprehensive Review.Clinical reviews in allergy & immunology · 2019Review
- Anaphylaxis Imaging: Non-Invasive Measurement of Surface Body Temperature and Physical Activity in Small Animals.PloS one · 2016Article
- Epitope analysis of Ara h 2 and Ara h 6: characteristic patterns of IgE-binding fingerprints among individuals with similar clinical histories.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2015Article
- Heterogeneous responses and cross reactivity between the major peanut allergens Ara h 1, 2,3 and 6 in a mouse model for peanut allergy.Clinical and translational allergy · 2015Article
- Generation of a canine anti-EGFR (ErbB-1) antibody for passive immunotherapy in dog cancer patients.Molecular cancer therapeutics · 2014Article
- Future Therapies for IgE-Mediated Food Allergy.Current pediatrics reports · 2014Article
- Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.Journal of agricultural and food chemistry · 2014Article
- The protein structure determines the sensitizing capacity of Brazil nut 2S albumin (Ber e1) in a rat food allergy model.Clinical and translational allergy · 2013Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPeanut allergy causes severe type 1 hypersensitivity reactions and conventional immunotherapy against peanut allergy is associated with a high risk of anaphylaxis.
objectiveOur current study reports proof of concept experiments on the safety of a stably denatured variant of the major peanut allergen Ara h 2 for immunotherapy. We determined the impact of structure loss of Ara h 2 on its IgE binding and basophil degranulation capacity, T cell reactivity as well as anaphylactic potential.
methodsThe secondary structure of untreated and reduced/alkylated Ara h 2 variants was determined by circular dichroism spectroscopy. We addressed human patient IgE binding to Ara h 2 by ELISA and Western blot experiments. RBL-SX38 cells were used to test the degranulation induced by untreated and reduced/alkylated Ara h 2. We assessed the anaphylactic potential of Ara h 2 variants by challenge of sensitized BALB/c mice. T cell reactivity was investigated using human Ara h 2-specific T cell lines and splenocytes isolated from sensitized mice.
resultsReduction/alkylation of Ara h 2 caused a decrease in IgE binding capacity, basophil degranulation and anaphylactic potential in vivo. However, the human T cell response to reduced/alkylated and untreated Ara h 2 was comparable. Mouse splenocytes showed higher metabolic activity upon stimulation with reduced/alkylated Ara h 2 and released similar IL-4, IL-13 and IFNγ levels upon treatment with either Ara h 2 variant. CONCLUSIONS AND CLINICAL RELEVANCE: Reduced/alkylated Ara h 2 might be a safer alternative than native Ara h 2 for immunotherapeutic treatment of peanut allergic patients.
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