ArticleThe Journal of biological chemistry2011
Structural and immunologic characterization of Ara h 1, a major peanut allergen.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 100 citations in OpenAlex.
- Magnetic Beads-Based Electrochemical Label-Free DNA-Bioassay for the Detection of Peanut Allergen Ara h2 in Food Matrices.Biosensors · 2026Article
- Identification and characterization of dietary antigens in oral tolerance.Science immunology · 2026Article
- Modeling Early Events in Food Sensitization: Complementary Insights from Caco-2 and T84 Epithelial Barriers Exposed to Peanut Allergens.Foods (Basel, Switzerland) · 2026Article
- Food Allergens of Plant Origin.Foods (Basel, Switzerland) · 2023Review
- Pea and lentil 7S globulin crystal structures with comparative immunoglobulin epitope mapping.Food chemistry. Molecular sciences · 2022Article
- Review
- Aptamer based point of care diagnostic for the detection of food allergens.Scientific reports · 2022Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- Ranking of 10 legumes according to the prevalence of sensitization as a parameter to characterize allergenic proteins.Toxicology reports · 2021Article
- Recent advances in the management of nut allergy.The World Allergy Organization journal · 2021Review
- Linking cross-reactivity clusters of food and respiratory allergens in PAMD@ to asthma and duration of allergy.The World Allergy Organization journal · 2020Article
- Crosslinked Recombinant-Ara h 1 Catalyzed by Microbial Transglutaminase: Preparation, Structural Characterization and Allergic Assessment.Foods (Basel, Switzerland) · 2020Article
- A proteomic analysis of peanut seed at different stages of underground development to understand the changes of seed proteins.PloS one · 2020Article
- Effects of different thermal processing methods on the structure and allergenicity of peanut allergen Ara h 1.Food science & nutrition · 2018Article
- Consumer-friendly food allergen detection: moving towards smartphone-based immunoassays.Analytical and bioanalytical chemistry · 2018Review
- Peanut allergens.Molecular immunology · 2018Review
- Jug r 6 is the allergenic vicilin present in walnut responsible for IgE cross-reactivities to other tree nuts and seeds.Scientific reports · 2018Article
- Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms.Scientific reports · 2016Article
- Lupin Peptides Modulate the Protein-Protein Interaction of PCSK9 with the Low Density Lipoprotein Receptor in HepG2 Cells.Scientific reports · 2016Article
- Immunotherapy using algal-produced Ara h 1 core domain suppresses peanut allergy in mice.Plant biotechnology journal · 2016Article
Corrections and comments
- Erratum issuedMattisohn, Christopher P [corrected to Mattison, Christopher P]
Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Allergic reactions to peanuts and tree nuts are major causes of anaphylaxis in the United States. We compare different properties of natural and recombinant versions of Ara h 1, a major peanut allergen, through structural, immunologic, and bioinformatics analyses. Small angle x-ray scattering studies show that natural Ara h 1 forms higher molecular weight aggregates in solution. In contrast, the full-length recombinant protein is partially unfolded and exists as a monomer. The crystal structure of the Ara h 1 core (residues 170-586) shows that the central part of the allergen has a bicupin fold, which is in agreement with our bioinformatics analysis. In its crystalline state, the core region of Ara h 1 forms trimeric assemblies, while in solution the protein exists as higher molecular weight assemblies. This finding reveals that the residues forming the core region of the protein are sufficient for formation of Ara h 1 trimers and higher order oligomers. Natural and recombinant variants of proteins tested in in vitro gastric and duodenal digestion assays show that the natural protein is the most stable form, followed by the recombinant Ara h 1 core fragment and the full-length recombinant protein. Additionally, IgE binding studies reveal that the natural and recombinant allergens have different patterns of interaction with IgE antibodies. The molecular basis of cross-reactivity between vicilin allergens is also elucidated.
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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.