Lupine allergy: Not simply cross-reactivity with peanut or soy

Peeters, Kim A.B.M.; Nordlee, Julie A.; Penninks, André; Chen, Lingyun; Goodman, Richard E.; Bruijnzeel-Koomen, Carla A.F.M.; Hefle, S.L.; Taylor, Steve L.; Knulst, André C.

doi:10.1016/j.jaci.2007.05.032

Cited by 68 publications

(81 citation statements)

References 25 publications

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“…However, cases of allergic reactions following lupin consumption as a bread ingredient or as snacks were reported in subjects with no prior allergy to peanut and negative SPT for this food (Smith et al, 2004;Peeters et al, 2007;Quaresma et al, 2007). This is corroborated by specific binding of IgE from sensitised individuals to isolated lupin globulins (Klos et al, 2010).…”

Section: Prevalencementioning

confidence: 99%

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

Products¹

2014

EFS2

115

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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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Section: Prevalencementioning

confidence: 99%

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

Products¹

2014

EFS2

115

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“…Although, the majority of edible legume grains and seed proteins from lupin species can cause allergy in a small percentage of the population, lupin products are increasingly included in human food, especially in Europe where lupin was approved as a food ingredient in 1997. 'Lupin allergy' occurs either separately or together with peanut allergy or allergy to other legumes [9]. Peanut-lupin cross allergy has been reported in which IgE antibodies recognize peanut allergens and also cross react with NLL conglutins [10].…”

Section: Introductionmentioning

confidence: 99%

Narrow‐leafed lupin (Lupinus angustifolius L.) β‐conglutin proteins modulate the insulin signaling pathway as potential type 2 diabetes treatment and inflammatory‐related disease amelioration

Lima-Cabello

Alché

Foley

et al. 2017

Molecular Nutrition Food Res

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The use of narrow leafed lupin -NLL (Lupinus angustifolius L.) as a new food is resulting in an increasing number of allergic reactions cases, particularly in atopic patients with other pre-existing legume allergies.In the current study, we have performed an extensive in silico analysis of the NLL seed β-conglutin proteins, a new family of major allergen proteins identified in NLL, and a comparison to other relevant food allergens such as peanut Ara h 1. We analysed the variability of surface residues involved in conformational IgE-binding epitopes, lineal B-and T-cell epitopes, and changes in 2-D structural elements and 3D motives, with the aim to investigate cross-allergenicity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes differential variability. Thus, variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-allergenicity among legumes.

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“…However, similar effects may also be caused by other lupin proteins characterised by different molecular weight, i.e., 13 kDa [6], 29 kDa [11], 34 kDa [12], 38 kDa [8], and 66 kDa [13]. The large heterogeneity of lupin seed proteins that exhibits Abstract Lupin seeds are already widely used as an ingredient in different food products.…”

Section: Introductionmentioning

confidence: 99%