Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy?

Peeters, Kim A.B.M.; Koppelman, Stef J.; Hoffen, Els van; Tas, C.W.H. van der; Jäger, Cornelie; Penninks, André; Hefle, Susan L.; Bruijnzeel-Koomen, Carla A.F.M.; Knol, Edward F.; Knulst, André C.

doi:10.1111/j.1365-2222.2006.02628.x

Cited by 119 publications

(111 citation statements)

References 32 publications

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“…This would require clinical investigations, studies in validated animal models, or in cell-based ex-vivo methods, all of which are beyond the scope of the current study. Nevertheless, a clinical study carried out by Peeters et al has shown that Ara h 2 and Ara h 6 are the most potent peanut allergens (Peeters et al, 2007), and our observation that the levels of these particular allergens do not differ substantially between the peanut types suggests that the in vivo allergenicity of the peanut types will also be comparable.…”

Section: Consequences For Allergenicitymentioning

confidence: 77%

“…A clinical study applying skin-prick tests demonstrated that peanut allergens Ara h 2 and Ara h 6 are 100-to 1000-fold more potent than Ara h 1 and Ara h 3 (Peeters et al, 2007), and it is therefore important to closely evaluate Ara h 2 and Ara h 6 specifically. Even though these allergens are less abundant (around 6% each, together approximately 12% of the total protein in peanut) compared to Ara h 1 and Ara h 3 (about 17% and 71%, respectively; Table 1), they may dominate the allergenic potential of peanut protein.…”

Section: Quantification Of Major Allergens Ara H 1 Ara H 2 Ara H 3mentioning

confidence: 99%

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Allergenicity attributes of different peanut market types

Koppelman

Jayasena

Luykx

et al. 2016

Food and Chemical Toxicology

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a b s t r a c tFour different market classes of peanut (Runner, Virginia Spanish, and Valencia) are commonly consumed in Western countries, but for some consumers peanuts are a main cause of food-induced anaphylaxis. Limited information is available on the comparative allergenicity of these distinct market classes. The aim of this study was to compare allergenicity attributes of different peanut cultivars.The protein content and protein profiles were highly comparable for all tested cultivars. All cultivar samples contained the major allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6, as assessed by SDS-PAGE and RP-HPLC, although some minor differences in major allergen content were found between samples. All samples were reactive in commercial ELISAs for detection and quantification of peanut protein. IgEbinding potency differed between samples with a maximum factor of 2, indicating a highly comparable allergenicity.Based on our observations, we conclude that peanuts from the main market types consumed in Western countries are highly comparable in their allergenicity attributes, indicating that safety considerations with regard to peanut allergy are not dependent on the peanut cultivar in question.

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Section: Consequences For Allergenicitymentioning

confidence: 77%

Section: Quantification Of Major Allergens Ara H 1 Ara H 2 Ara H 3mentioning

confidence: 99%

Allergenicity attributes of different peanut market types

Koppelman

Jayasena

Luykx

et al. 2016

Food and Chemical Toxicology

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“…However, only a few comparative SPT studies with purified food allergens have been conducted, [28], [72], [73] and [74] which is mainly due to the high demands of approval in clinical trials as requested by the institutional review boards and regulatory authorities to ensure patient safety (test allergens have to be licensed as biotechnologic products). These few studies verified a superior diagnostic potential of recombinant allergens.…”

Section: Skin Tests With Purified Allergenic Moleculesmentioning

confidence: 99%

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Steckelbroeck¹,

Ballmer‐Weber²,

Vieths³

2008

Journal of Allergy and Clinical Immunology

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This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both. However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both.However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. IgE-mediated and non-IgE-mediated syndromes, where IgE-mediated manifestations are responsible for the majority of food-induced, immediate-type, immune-mediated hypersensitivity reactions. 3 The development of an IgE-mediated response to food requires a series of molecular and cellular interactions, which involve antigenpresenting cells, T lymphocytes, and B lymphocytes. [4] and [5] Depending on the route of sensitization, food allergy is the result of either genuine reactivity to comestibles through the gastrointestinal tract (class I food allergens) or secondary sensitization to cross-reactive food allergens as a consequence of the initial reactivity to homologous pollen-related allergens (class II food allergens). [6] and [7] The majority of class I food allergens are heat stable and resistan...

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“…This was confirmed by doubleblind placebo-controlled oral challenge and the authors concluded that this was not due to a primary sensitization, but due to cross-reactivity with aero-allergens. Lupin was introduced into the food chain in the late nineties in the EU (Peeters et al, 2007). According to Hieta et al (2009), allergic reactions to lupin occurred most frequently among patients with other food allergies, mainly to legumes, indicating that lupin allergy occurs largely due to cross-reactivity.…”

Section: Allergenicity Risk Assessmentmentioning

confidence: 99%

“…According to Hieta et al (2009), allergic reactions to lupin occurred most frequently among patients with other food allergies, mainly to legumes, indicating that lupin allergy occurs largely due to cross-reactivity. However, others showed that lupin allergy is not always due to cross-reactivity, but can be the result of primary sensitization through oral exposure (Lindvik et al, 2008;Peeters et al, 2007), and also by prior inhalation of lupin flour (Prieto et al, 2010). Similar to lupin, kiwi fruit was introduced to the EU in the 20th century and soon after kiwi allergy was first reported (Fine, 1981).…”

Section: Allergenicity Risk Assessmentmentioning

confidence: 99%

Approaches to assess IgE mediated allergy risks (sensitization and cross-reactivity) from new or modified dietary proteins

Remington¹,

Broekman

Blom³

et al. 2018

Food and Chemical Toxicology

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A B S T R A C TThe development and introduction of new dietary protein sources has the potential to improve food supply sustainability. Understanding the potential allergenicity of these new or modified proteins is crucial to ensure protection of public health. Exposure to new proteins may result in de novo sensitization, with or without clinical allergy, or clinical reactions through cross-reactivity.In this paper we review the potential of current methodologies (in silico, in vitro degradation, in vitro IgE binding, animal models and clinical studies) to address these outcomes for risk assessment purposes for new proteins, and especially to identify and characterise the risk of sensitization for IgE mediated allergy from oral exposure. Existing tools and tests are capable of assessing potential crossreactivity. However, there are few possibilities to assess the hazard due to de novo sensitization. The only methods available are in vivo models, but many limitations exist to use them for assessing risk. We conclude that there is a need to understand which criteria adequately define allergenicity for risk assessment purposes, and from these criteria develop a more suitable battery of tests to distinguish between proteins of high and low allergenicity, which can then be applied to assess new proteins with unknown risks.

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Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy?

Abstract: Ara h 2 and Ara h 6 appeared to be more potent than Ara h 1 and Ara h 3. Both SPT reactivity to low concentrations of Ara h 2 and Ara h 6 and to higher concentrations of Ara h 1 and Ara h 3 were shown to be indicative of severe symptoms.

Cited by 119 publications

References 32 publications

Allergenicity attributes of different peanut market types

Allergenicity attributes of different peanut market types

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Approaches to assess IgE mediated allergy risks (sensitization and cross-reactivity) from new or modified dietary proteins

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