We recommend the following for sandwich ELISA (Capture - Detection): HMABPY117 - HMABPY117D
Target
Alternative Names
Ara h 2; Peanut allergen Ara H2
Citations
Publication ()
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Background
Peanut allergy (PNA) is mediated by IgE, which has attracted much attention because of the severity of the reaction and the increasing incidence and incidence of anaphylactic shock. Symptoms of peanut allergy can manifest in multiple organs, including the mouth, skin, gastrointestinal tract, cardiovascular and respiratory systems, and in severe cases can be life-threatening. Peanut allergy is common in younger age groups, and about 25% of children with food allergies in the United States are allergic to peanuts. The prevalence of peanut allergy has increased several-fold compared to the past, and peanut allergy accounts for the majority of severe food-related allergic reactions and carries the highest lifetime risk of anaphylaxis and anaphylactic shock death, with even exposure to trace amounts of peanuts causing severe reactions.
Sixteen peanut allergens have been identified, ranging from Arachis hypogaea 1 (Ara h 1) to Ara h 17 (excluding Ara h 4). People in different regions have different sensitization patterns to peanut allergens. The results of the study found that peanut allergens causing allergic reactions differed according to geographic location, for example, the peanut allergens Ara h 1, Ara h 2, and Ara h 3 were the main sensitizers causing allergic reactions in children in the United States, whereas patients in Spain were sensitized to Ara h 9 at a higher rate. Ara h 2 is a 2S albumin storage protein, which belongs to the gliadin superfamily and contains two isomers. Ara h 2 can be purified to a dimer, and both bands have the same N-terminal sequence, which can be hydrolyzed by peanut protease to remove the C-terminal dipeptide. Therefore, Ara h 2 is not only a mixture of two isomers, but also a slightly truncated form of two isomers.
Figure 1. Ribbon representations of the known structures of peanut allergens (Source: Palladino C, et al. 2018)
The clinical diagnosis of peanut allergy mainly depends on clinical examination and laboratory testing. Asking for a medical history may be sufficient to diagnose PNA for those patients with typical peanut allergy, while it is necessary for patients without a clear medical history to take further testing to determine PNA. It is believed that the combined applications of component-resolved diagnosis, basophil activation test, IgE epitope mapping, and high-throughput microarray platform may be the detection method for PNA in the future, which can improve the accuracy of diagnosis and prognosis.
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References
Design of an Ara h 2 hypoallergen from conformational epitopes
Clin Exp Allergy
Authors: Min J, Keswani T, LaHood NA, Lytle IR, Marini-Rapoport O, Andrieux L, Sneed SL, Edwards LL, Petrovich RM, Perera L, Pomés A, Pedersen LC, Patil SU, Mueller GA.
Introduction: Adverse reactions are relatively common during peanut oral immunotherapy. To reduce the risk to the patient, some researchers have proposed modifying the allergen to reduce IgE reactivity, creating a putative hypoallergen. Analysis of recently cloned human IgG from patients treated with peanut immunotherapy suggested that there are three common conformational epitopes for the major peanut allergen Ara h 2. We sought to test if structural information on these epitopes could indicate mutagenesis targets for designing a hypoallergen and evaluated the reduction in IgE binding via immunochemistry and a mouse model of passive cutaneous anaphylaxis (PCA).
Methods: X-ray crystallography characterized the conformational epitopes in detail, followed by mutational analysis of key residues to modify monoclonal antibody (mAb) and serum IgE binding, assessed by ELISA and biolayer interferometry. A designed Ara h 2 hypoallergen was tested for reduced vascularization in mouse PCA experiments using pooled peanut allergic patient serum.
Results: A ternary crystal structure of Ara h 2 in complex with patient antibodies 13T1 and 13T5 was determined. Site-specific mutants were designed that reduced 13T1, 13T5, and 22S1 mAbs binding by orders of magnitude. By combining designed mutations from the three major conformational bins, a hexamutant (Ara h 2 E46R, E89R, E97R, E114R, Q146A, R147E) was created that reduced IgE binding in serum from allergic patients. Further, in the PCA model where mice were primed with peanut allergic patient serum, reactivity upon allergen challenge was significantly decreased using the hexamutant.
Conclusion: These studies demonstrate that prior knowledge of common conformational epitopes can be used to engineer reduced IgE reactivity, an important first step in hypoallergen design.
The combination of Ara h 2-sIgE and basophil activation test could be an alternative to oral food challenge in cases of suspected peanut allergy
Pediatr Allergy Immunol
Authors: Carrette M, Couderc L, Bubenheim M, Vidal A, Youssouf A, Boyer O, Marguet C, Martinet J.
Background: Most children with peanut sensitisation do not have a clinical peanut allergy (PA). Oral food challenge (OFC) is then necessary to diagnose PA and assess the reactive dose of the allergen. However, OFC is laborious to perform, expensive and stressful. We evaluated whether in vitro tests, such as basophil activation test (BAT), allergen-specific IgE (sIgE) and their combination, could be used to replace OFC for the diagnosis of PA in children.
Methods: Ninety-one patients aged 6 months to 18 years with suspected PA were prospectively recruited. These patients then underwent an OFC to assess PA. Whole peanut-sIgE, Ara h 2-sIgE, Ara h 8-sIgE and %CD63+ basophils (CCR3+ /SCClow ) to peanut measured by BAT were investigated for PA diagnosis.
Results: Forty-one patients had a positive peanut OFC, and the remaining 50 were only sensitised. All patients with Ara h 2-sIgE >7 kUA /L were allergic to peanut. A threshold of 6% for activated basophils yielded a sensitivity of 95% and a specificity of 54%. All patients with Ara h 2-sIgE ≤7 kUA /L and BAT ≤6% (n = 22) had a negative OFC except for one who presented an oral syndrome due to PR-10 sensitisation.
Conclusions: We have shown that Ara h 2-sIgE >7 kUA/L is a discriminating threshold for the diagnosis of PA. Furthermore, when Ara h 2-sIgE ≤7 kUA/L and BAT ≤6%, patients do not need to adjust their diet and, thus, do not need an OFC.
COA
Publication 
Figure 1. Ribbon representations of the known structures of peanut allergens
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