The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms

Lewis, Stuart; Grimshaw, Kate; Warner, J. O.; Hourihane, Jonathan

doi:10.1111/j.1365-2222.2005.02252.x

Cited by 66 publications

(53 citation statements)

References 28 publications

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“…2) a predominant role of this protein in the allergenic response to lupin, which is in agreement with previous reports (Holden et al, 2008;Moneret-Vautrin et al, 1999). Moreover, the protein alignments have shown that the IgE-binding lupin peptides from a-conglutin and b-conglutin are highly homologous to allergic peanut peptides reported in literature (Lewis et al, 2005;van Boxtel et al, 2008), highlighting several conserved epitopes recognised by IgE antibodies. In a recent work of our group a lupin protein isolate was submitted to industrial food processing with the aim to study the change of the protein bio-availability before and after strong thermal treatments (Sirtori et al, 2010).…”

Section: Discussionsupporting

confidence: 88%

“…The peptides identified in the reactive spots were aligned against known allergenic peptides (Lewis, Grimshaw, Warner, & Hourihane, 2005;van Boxtel, Koppelman, van den Broek, & Gruppen, 2008) belonging to the major peanut allergens. Supplementary Table IV summarises the results of the alignments obtained with the BLASTp Program: allergen Ara h 1 was aligned against b-conglutin precursor, vicilin-like protein and b-conglutin showing an identity between 50% and 76% and a homology between 63% and 93%.…”

Section: Identification Of Reactive Lupin Proteins By Western Blottinmentioning

confidence: 99%

See 1 more Smart Citation

Cross-reactivity between peanut and lupin proteins

Sirtori

Resta²,

Arnoldi

et al. 2011

Food Chemistry

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Section: Discussionsupporting

confidence: 88%

Section: Identification Of Reactive Lupin Proteins By Western Blottinmentioning

confidence: 99%

Cross-reactivity between peanut and lupin proteins

Sirtori

Resta²,

Arnoldi

et al. 2011

Food Chemistry

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“…Peeters et al 78 used purified peanut proteins (Ara h 1-3, Ara h 6) and found a correlation of clinical severity with recognition of Ara h 2 and 6 at low concentrations, and Ara h 1 and 3 at higher concentrations, indicating apparent increased potency of Ara h 2, also noted by Palmer et al 79 Astier et al 80 used recombinant peanut proteins, recombinant Ara h 1-3, and found binding was dominant to recombinant Ara h 2, but severity correlated with polysensitization. Indeed, a positive correlation of reaction severity with increased diversity of binding, whether to the allergens 78,81 or epitopes, 82 is a common theme that may translate to future diagnostic tests that can predict severity, likelihood of current allergy, and resolution.…”

Section: Present and Future Diagnostic Strategies/natural Coursementioning

confidence: 97%

Peanut allergy: Emerging concepts and approaches for an apparent epidemic

Sicherer

Sampson

2007

Journal of Allergy and Clinical Immunology

301

223

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“…Four studies (Hourihane et al, 1997;Wensing Marjolein et al, 2002;Lewis et al, 2005;Flinterman et al, 2006a) were specifically designed to assess LOAEL doses and provide accurate information on the doses tested (Taylor et al, 2009b).…”

Section: Minimum (Observed) Eliciting Dosesmentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

101

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Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

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The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms

Cited by 66 publications

References 28 publications

Cross-reactivity between peanut and lupin proteins

Cross-reactivity between peanut and lupin proteins

Peanut allergy: Emerging concepts and approaches for an apparent epidemic

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

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