IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3

Bublin, Merima; Kostadinova, Maria; Radauer, Christian; Häfner, Christine; Szépfalusi, Zsolt; Varga, Eva‐Maria; Maleki, Soheila J.; Hoffmann‐Sommergruber, Karin; Breiteneder, Heimo

doi:10.1016/j.jaci.2013.01.022

Cited by 84 publications

(94 citation statements)

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“…All but 1 of the patients who were sensitized to Ara h 2 and Ara h 6 showed concomitant sensitization to Ara h 1 and/or Ara h 3. Our findings are in line with others showing that Ara h 2 is the most important peanut allergen [1,2,3,4,5,6,11,21,22]. Data about the prevalence and diagnostic value of Ara h 6 are rare, but in accordance with our results two studies showed that both peanut 2S albumins are recognized by IgE from the same patients in almost all cases and that the diagnostic accuracy of IgE specific to Ara h 6 in adults is as good as for Ara h 2 [1,7].…”

Section: Discussionsupporting

confidence: 93%

Component-Resolved IgE Profiles in Austrian Patients with a Convincing History of Peanut Allergy

Ackerbauer

Bublin

Radauer

et al. 2015

Int Arch Allergy Immunol

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Background: Peanut allergy develops after primary sensitization to peanut allergens and/or IgE cross-sensitization with homologous allergens from various plants. Therefore, heterogeneous patterns of sensitization to individual peanut allergens are observed in different countries. The aim of this study was to examine the IgE sensitization patterns of Austrian peanut-allergic patients. Methods: Sera from 65 peanut-allergic patients and 20 peanut-tolerant atopics were obtained in four Austrian allergy clinics.Sensitization patterns against peanut allergens Ara h 1-3, 6, 8 and 9 were identified by ImmunoCAP and ImmunoCAP ISAC. Results: Austrian peanut-allergic patients were sensitized to Ara h 2 and 6 (71%), followed by Ara h 1 (62%), Ara h 8 (45%), Ara h 3 (35%) and Ara h 9 (11%). All sera containing Ara h 2-specific IgE were also positive for Ara h 6, with Ara h 6-specific IgE levels significantly (p < 0.05) higher compared with Ara h 2. Twelve percent displayed IgE reactivity exclusively to Ara h 8. Peanut extract and Ara h 8 showed low diagnostic specificities of 25 and 10%, respectively. The other peanut allergens showed 100% specificity. Diagnostic sensitivities determined by ImmunoCAP ISAC and ImmunoCAP were highly similar for Ara h 2, 3 and 8. Conclusions: Themajority of symptomatic peanut-allergic patients are sensitized to Ara h 2 and Ara h 6. In peanut-symptomatic patients with additional birch pollen allergy, other peanut allergens, especially Ara h 8, should be tested when IgE reactivity to Ara h 2 is absent.

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Section: Discussionsupporting

confidence: 93%

Component-Resolved IgE Profiles in Austrian Patients with a Convincing History of Peanut Allergy

Ackerbauer

Bublin

Radauer

et al. 2015

Int Arch Allergy Immunol

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“…The eight epitopes identified for Ara h 2, that are similar to those previously reported, include the epitopes that have been recently shown to be responsible for cross-reactivity with Ara h 1 and Ara h 3 [38, 46, 49]. Seven epitopes were newly identified for Ara h 6 (Fig.…”

Section: Discussionsupporting

confidence: 76%

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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“…We were able to establish 2 ELISA systems for the reliable determination of Ara h 2 and Ara h 6 in the complex breast milk matrix without any relevant cross-reactivity against single allergens and extracts which have been selected for structural similarities, sequence identities, and a phylogenetic relationship. The included allergens and allergen sources for cross-reactivity studies were chosen according to their structure similarities with Ara h 2 and Ara h 6, which are the cross-reactive counterparts Ara h 6 and Ara h 2, respectively, the α-amylase-inhibitor [27], and the peanut allergen Ara h 1, which was described as being IgE cross-reactive because of high sequence similarity on surface-exposed loops [28]. However, none of the investigated allergens were detected by the newly developed Ara h 2 and Ara h 6 sandwich ELISAs.…”

Section: Discussionmentioning

confidence: 99%

Detection of the Peanut Allergens Ara h 2 and Ara h 6 in Human Breast Milk: Development of 2 Sensitive and Specific Sandwich ELISA Assays

Schocker

Scharf

Kull

et al. 2017

Int Arch Allergy Immunol

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Background: Little is known about breast milk as a vehicle for tolerance development or sensitization to peanuts very early in life. Thus, well-characterized and highly sensitive detection systems for the reliable determination of peanut allergens in breast milk are mandatory. Methods: For the quantification of the marker allergens Ara h 2 and Ara h 6 in the low nanogram per milliliter range in breast milk samples of a German cohort, sensitive and highly specific sandwich ELISAs were optimized and validated. Results: The Ara h 2 ELISA revealed a limit of detection (LOD) of 1.3 ng Ara h 2/mL and a quantification range of 2.3-250 ng/mL, the Ara h 6 ELISA showed an LOD of 0.7 ng/mL and a working range of 1.1-14.4 ng/mL. The assays showed no relevant cross-reactivity against other potentially cross-reactive legume, seed, and tree nut extracts (<0.01%, except for Ara h 1 in the Ara h 2 ELISA <0.1%). Ara h 2 was detectable in breast milk samples from 14/40 (35%) of the participants in concentrations from 2.3 to 184 ng/mL, Ara h 6 appeared in 9/40 (22.5%) of the lactating mothers between 1.1 and 9.7 ng/mL, and 1 highly positive sample with 79 ng/mL. Both allergens appeared at the same time points, but Ara h 6 in lower concentrations than Ara h 2. Conclusions: Sensitive and specific diagnostic tools for the determination of Ara h 2 and Ara h 6 in human breast milk were established. The kinetics of secreted Ara h 2 and Ara h 6 seem to be similar but with a difference in concentration. Follow-up investigations on their tolerogenic or sensitizing properties in breast milk become now accessible.

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IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3

Abstract: Occurrence of similar sequences in the 3 major peanut allergens accounts for the high extent of cross-reactivity among them.

Cited by 84 publications

References 43 publications

Component-Resolved IgE Profiles in Austrian Patients with a Convincing History of Peanut Allergy

Component-Resolved IgE Profiles in Austrian Patients with a Convincing History of Peanut Allergy

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 Allergens Ara h 2 and Ara h 6 in Human Breast Milk: Development of 2 Sensitive and Specific Sandwich ELISA Assays

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