Ara h 6 Complements Ara h 2 as an Important Marker for IgE Reactivity to Peanut

Koid, Audrey; Chapman, Martin D.; Hamilton, Robert G.; Ree, Ronald van; Versteeg, Serge A.; Dreskin, Stephen C.; Koppelman, Stef J.; Wünschmann, Sabina

doi:10.1021/jf4022509

Cited by 40 publications

(36 citation statements)

References 55 publications

(158 reference statements)

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“…177 Ara h 2 and Ara h 6 are the most clinically relevant allergens in peanut allergy. 178,179 Ara h 1 (7S globulin) and Ara h 3 (11S globulin) are seed proteins belonging to the cupin superfamily, which contains a conserved barrel domain. 180,181 Ara h 5 is a member of the profilin family with 72% AA sequence identity to birch pollen profilin (Bet v 2), and is a class II type labile food allergen.…”

Section: Sarcoplasmic Calcium-binding Proteinmentioning

confidence: 99%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

202

135

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Food allergy is an adverse immune response to certain kinds of food. Although any food can cause allergic reactions, chicken egg, cow's milk, wheat, shellfish, fruit, and buckwheat account for 75% of food allergies in Japan. Allergen-specific immunoglobulin E (IgE) antibodies play a pivotal role in the development of food allergy. Recent advances in molecular biological techniques have enabled the efficient analysis of food allergens. As a result, many food allergens have been identified, and their molecular structure and IgE-binding epitopes have also been identified. Studies of allergens have demonstrated that IgE antibodies specific to allergen components and/or the peptide epitopes are good indicators for the identification of patients with food allergy, prediction of clinical severity and development of tolerance. In this review, we summarize our current knowledge regarding the allergens and IgE epitopes in the well-researched allergies to chicken egg, cow's milk, wheat, shrimp, and peanut.

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Section: Sarcoplasmic Calcium-binding Proteinmentioning

confidence: 99%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

202

135

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“…Of these, two 2S albumins, Ara h 2 and Ara h 6, together account for approximately 10% of the peanut proteome and are recognized by IgE from most peanut-allergic children and adults [9, 10]. Ara h 2 and Ara h 6 are moderately homologous in both their primary and secondary structure (4 and 5 disulphide bonds, respectively), are the most potent peanut allergens, and are substantially redundant in their biologic activity [11–21].…”

Section: Introductionmentioning

confidence: 99%

Epitope analysis of Ara h 2 and Ara h 6: characteristic patterns of IgE‐binding fingerprints among individuals with similar clinical histories

Otsu

Guo

Dreskin

2015

Clin Experimental Allergy

101

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Summary Background Ara h 2 and Ara h 6 are moderately homologous and highly potent peanut allergens. Objective To identify IgE-binding linear epitopes of Ara h 6, compare them to those of Ara h 2, and to stratify binding based on clinical histories. Methods Thirty highly peanut-allergic subjects were stratified by clinical history. Sera were diluted to contain the same amount of anti-peanut IgE. IgE binding to overlapping 20-mer peptides of Ara h 2 and Ara h 6 was assessed using microarrays. Results Each subject had a unique IgE-binding fingerprint to peptides; these data were coalesced into epitope binding. IgE from subjects with a history of more severe reactions (n = 19) had a smaller frequency of binding events (BEs) for both Ara h 2 (52 BEs of 152 (19×8epitopes) possible BEs and Ara h 6 (13 BEs of 133 (19×7 epitopes) possible BEs) compared to IgE from those with milder histories (n = 11) (Ara h 2: 47 BEs of 88 (11×8 epitopes) possible BEs, P < 0.01; Ara h 6: 25 BEs of 77 (11×7 epitopes) possible BEs, P < 0.001). Using an unsupervised hierarchal cluster analysis, subjects with similar histories tended to cluster. We have tentatively identified a high-risk pattern of binding to peptides of Ara h 2 and Ara h 6, predominantly in subjects with a history of more severe reactions (OR = 12.6; 95% CI: 2.0–79.5; P < 0.01). Conclusions and Clinical Relevance IgE from patients with more severe clinical histories recognize fewer linear epitopes of Ara h 2 and Ara h 6 than do subjects with milder reactions and bind these epitopes in characteristic patterns. Close examination of IgE binding to epitopes of Ara h 2 and Ara h 6 may have prognostic value.

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“…More recently, Ara h 6 also emerged as an important allergen since it has a similar seroprevalence to Ara h 2 and has also been associated to clinical peanut allergy. Ara h 6 (14.5 kDa) is a conglutin (2S albumin) with heat-stable and immunogenic properties, being resistant to gut digestion [7,8]. Due to its stability, Ara h 6 can be considered a suitable marker to identify the presence of peanut in food products and production lines.…”

Section: Introductionmentioning

confidence: 99%

Detection of the peanut allergen Ara h 6 in foodstuffs using a voltammetric biosensing approach

et al. 2015

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A voltammetric biosensor for Ara h 6 (a peanut allergen) detection in food samples was developed. Gold nanoparticle-modified screen-printed carbon electrodes were used to develop a sandwich-type immunoassay using twomonoclonal antibodies. The antibody-antigen interaction was detected through the electrochemical detection of enzymatically deposited silver. The immunosensor presented a linear range between 1 and 100 ng/ml, as well as high precision (inter-day RSD ≤9.8 %) and accuracy (recoveries ≥96.7 %). The detection and quantification limits were 0.27 and 0.88 ng/ml, respectively. It was possible to detect small levels of Ara h 6 in complex food matrices.

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Ara h 6 Complements Ara h 2 as an Important Marker for IgE Reactivity to Peanut

Cited by 40 publications

References 55 publications

Common food allergens and their IgE-binding epitopes

Common food allergens and their IgE-binding epitopes

Epitope analysis of Ara h 2 and Ara h 6: characteristic patterns of IgE‐binding fingerprints among individuals with similar clinical histories

Detection of the peanut allergen Ara h 6 in foodstuffs using a voltammetric biosensing approach

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