ArticleAllergy2013
Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products.
Article in Allergy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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
22 citing papers in PubMed, 73 citations in OpenAlex.
- Intestinal permeability, food antigens and the microbiome: a multifaceted perspective.Frontiers in allergy · 2024Review
- Food allergy: cause or consequence of pediatric eosinophilic esophagitis? Potential implications of ultraprocessed foods in prevention and management.Frontiers in allergy · 2023Review
- Do advanced glycation end products contribute to food allergy?Frontiers in allergy · 2023Review
- Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting.Foods (Basel, Switzerland) · 2022Article
- Reduction in Allergenicity and Induction of Oral Tolerance of Glycated Tropomyosin from Crab.Molecules (Basel, Switzerland) · 2022Article
- Maillard Reaction Induced Changes in Allergenicity of Food.Foods (Basel, Switzerland) · 2022Review
- Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy.Nutrients · 2022Review
- Human monocyte-derived type 1 and 2 macrophages recognize Ara h 1, a major peanut allergen, by different mechanisms.Scientific reports · 2021Article
- Interaction of Monocyte-Derived Dendritic Cells with Ara h 2 from Raw and Roasted Peanuts.Foods (Basel, Switzerland) · 2020Article
- Contribution of Chemical Modifications and Conformational Epitopes to IgE Binding by Ara h 3.Foods (Basel, Switzerland) · 2018Article
- Effects of different thermal processing methods on the structure and allergenicity of peanut allergen Ara h 1.Food science & nutrition · 2018Article
- Review
- Food Processing: The Influence of the Maillard Reaction on Immunogenicity and Allergenicity of Food Proteins.Nutrients · 2017Review
- Immunotherapy using algal-produced Ara h 1 core domain suppresses peanut allergy in mice.Plant biotechnology journal · 2016Article
- Enhanced Approaches for Identifying Amadori Products: Application to Peanut Allergens.Journal of agricultural and food chemistry · 2016Article
- In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides.Food science & nutrition · 2015Article
- Glycoproteomic analysis of seven major allergenic proteins reveals novel post-translational modifications.Molecular & cellular proteomics : MCP · 2015Article
- Article
- Purification of Recombinant Peanut Allergen Ara h 1 and Comparison of IgE Binding to the Natural Protein.Foods (Basel, Switzerland) · 2014Article
- Dry roasting enhances peanut-induced allergic sensitization across mucosal and cutaneous routes in mice.The Journal of allergy and clinical immunology · 2014Article
Corrections and comments
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Authors and funding
15 authors at 7 institutions in 1 country.
Funding
Abstract
backgroundRecent immunological data demonstrated that dendritic cells preferentially recognize advanced glycation end product (AGE)-modified proteins, upregulate expression of the receptor for AGE (RAGE), and consequently bias the immune response toward allergy.
methodsPeanut extract was characterized by mass spectrometry (MS) to elucidate the specific residues and specific AGE modifications found in raw and roasted peanuts and on rAra h 1 that was artificially glycated by incubation with glucose or xylose. The binding of the RAGE-V1C1 domain to peanut allergens was assessed by PAGE and Western analysis with anti-Ara h 1, 2, and 3 antibodies. IgE binding to rAra h 1 was also assessed using the same methods.
resultsAGE modifications were found on Ara h 1 and Ara h 3 in both raw and roasted peanut extract. No AGE modifications were found on Ara h 2. Mass spectrometry and Western blot analysis demonstrated that RAGE binds selectively to Ara h 1 and Ara h 3 derived from peanut extract, whereas the analysis failed to demonstrate Ara h 2 binding to RAGE. rAra h 1 with no AGE modifications did not bind RAGE; however, after AGE modification with xylose, rAra h 1 bound to RAGE.
conclusionsAGE modifications to Ara h 1 and Ara h 3 can be found in both raw and roasted peanuts. Receptor for AGE was demonstrated to selectively interact with AGE-modified rAra h 1. If sensitization to peanut allergens occurs in dendritic cells via RAGE interactions, these cells are likely interacting with modified Ara h 1 and Ara h 3, but not Ara h 2.
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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.