Component‐resolved diagnostics for the evaluation of peanut allergy in a low‐prevalence area

Suratannon, Narissara; Ngamphaiboon, Jarungchit; Wongpiyabovorn, Jongkonnee; Puripokai, Panitchaya; Chatchatee, Pantipa

doi:10.1111/pai.12125

Cited by 29 publications

(32 citation statements)

References 34 publications

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“…Interestingly, the two studies with a positive LR+ and negative LRÀ for both sIgE to Ara h 8 and Ara h 9 were the two studies performed in Asian populations [14,25]. A negative LR+ and positive LRÀ was found in three of five studies analysing sIgE to Ara h 8 and two of four studies analysing sIgE to Ara h 9, indicating that a value above the cutoff value was suggestive for peanut tolerance.…”

Section: Sige To Peanut Componentsmentioning

confidence: 95%

Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review

Klemans

Os‐Medendorp

Blankestijn

et al. 2015

Clin Experimental Allergy

105

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The diagnostic accuracy of skin prick test (SPT) and specific IgE (sIgE) to peanut extract in diagnosing peanut allergy is suboptimal. Recent studies have evaluated sIgE to peanut components as a possible new diagnostic tool. The aim of our review was to systematically search the literature to assess the diagnostic value of sIgE to peanut components in diagnosing peanut allergy. A literature search was performed in PubMed, Embase and the Cochrane Library. Results were subsequently screened for in- and exclusion criteria. The quality of eligible studies was assessed using a standardized quality assessment tool (QUADAS-2). Data on sensitivity, specificity, and positive and negative likelihood ratios were extracted or calculated for a descriptive analysis. Twenty-two studies were eligible, of which 21 studies in paediatric populations. Most studies reported on sIgE to peanut extract (15) and sIgE to Ara h 2 (12), followed by SPT (9) and sIgE to Ara h 1 (7). All studies were at risk of bias or caused applicability concerns on at least one item of the quality assessment tool. The best combination of diagnostic accuracy measures of all diagnostic tests was found for sIgE to Ara h 2. This finding was independent of geographical location. Compared to SPT and sIgE to peanut extract, sIgE to Ara h 2 was mainly superior in diagnosing peanut allergy in case of a positive test result. Worst diagnostic accuracy measures were found in general for sIgE to Ara h 8 and sIgE to Ara h 9. sIgE to Ara h 2 showed the best diagnostic accuracy of all diagnostic tests to diagnose peanut allergy. Compared to the currently used SPT and sIgE to peanut extract, sIgE to Ara h 2 was superior in diagnosing peanut allergy and should therefore replace these tests in daily clinical practice, especially in children.

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Section: Sige To Peanut Componentsmentioning

confidence: 95%

Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review

Klemans

Os‐Medendorp

Blankestijn

et al. 2015

Clin Experimental Allergy

105

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“…CRD uses purified or recombinant allergens (such as rAra h 2) 98 to identify allergen-specific IgE and IgG4 antibodies 99 , which may distinguish various allergenic, non-allergenic and crossreactive molecules in standardized amounts. BATs are carried out using allergenic proteins as stimulants.…”

Section: Diagnostic Tests For Food Allergiesmentioning

confidence: 99%

Food allergy: immune mechanisms, diagnosis and immunotherapy

2016

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Food allergy is a pathological, potentially deadly, immune reaction triggered by normally innocuous food protein antigens. The prevalence of food allergies is rising and the standard of care is not optimal, consisting of food-allergen avoidance and treatment of allergen-induced systemic reactions with adrenaline. Thus, accurate diagnosis, prevention and treatment are pressing needs, research into which has been catalysed by technological advances that are enabling a mechanistic understanding of food allergy at the cellular and molecular levels. We discuss the diagnosis and treatment of IgE-mediated food allergy in the context of the immune mechanisms associated with healthy tolerance to common foods, the inflammatory response underlying most food allergies, and immunotherapy-induced desensitization. We highlight promising research advances, therapeutic innovations and the challenges that remain.

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“…It emerged that patterns of IgE binding to peanut proteins may vary according to geographical location [1,2,3,4,5,6,11,21,24]. Sensitization to Ara h 8 is more prominent in peanut-allergic patients exposed to pollen from Fagales trees, such as birch or alder, and, according to recent studies from Sweden, isolated Ara h 8 sensitization is a marker of a mild reaction if any [11,14].…”

Section: Discussionmentioning

confidence: 99%

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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Component‐resolved diagnostics for the evaluation of peanut allergy in a low‐prevalence area

Abstract: Our study identifies three allergen components: rAra h 2, rAra h 9, and CCD as important components in the diagnosis of peanut allergy in an Asian country with low prevalence. The ratio between rArah h 2 sIgE to peanut sIgE can be used for predicting patients who will develop anaphylaxis.

Cited by 29 publications

References 34 publications

Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review

Diagnostic accuracy of specific IgE to components in diagnosing peanut allergy: a systematic review

Food allergy: immune mechanisms, diagnosis and immunotherapy

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

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