Cross-reactivity between peanut and lupin proteins

Sirtori, E.; Resta, Donatella; Arnoldi, Anna; Savelkoul, H.F.J.; Wichers, Harry J.

doi:10.1016/j.foodchem.2010.11.073

Cited by 19 publications

(10 citation statements)

References 32 publications

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“…Lupine is increasingly recognized as a human health food as the grain is high in protein and dietary fiber, gluten‐free and low in fat, with virtually no starch and thus has a very low glycemic index (Sipsas, 2008). Potential benefits to human health for lupines include: satiety and reducing appetite for weight loss (Lee et al, 2006), bowel health (Johnson et al, 2006), hypocholesterolemic activity (Sirtori et al, 2004; Hall et al, 2005; Martins et al, 2005; Sirtori et al, 2011), reduced blood glucose and insulin response (Hall et al, 2005; Capraro et al, 2011), reduced blood pressure (Lee et al, 2009), and eye health (Fryirs et al, 2008). Lupines have a number of advantages over the market‐dominant protein grain, soybean, with respect to seed quality and nutrition for food end uses (Wolko et al, 2011).…”

Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

“…Allergenicity in lupines occurs either separately or together with peanut allergy or an allergy to other legume species (Peeters et al, 2007; Campbell and Yates, 2010; Jappe and Vieths, 2010). The estimates of peanut‐allergic individuals reacting also to lupine varies between 4% and 68% (Sirtori et al, 2011). Research on the allergenicity in lupines is underway, and it is expected that avenues will be identified to reduce this characteristic in lupine in the future (Goggin et al, 2008).…”

Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

“…Research on the allergenicity in lupines is underway, and it is expected that avenues will be identified to reduce this characteristic in lupine in the future (Goggin et al, 2008). Of the four major classes of storage protein so far identified in lupine, α, β, γ, and δ (Foley et al, 2011), it is unclear which one(s) is responsible for allergenicity, with different candidates identified in different studies (Magni et al, 2005; Goggin et al, 2008; Holden et al, 2008; Sirtori et al, 2011). These studies provide the basis for further work aiming to target allergen genes using RNA interference to reduce allergenicity (Singh and Bhalla, 2008).…”

Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

See 2 more Smart Citations

How a phosphorus‐acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae)

Lambers

Clements

Nelson

2013

American J of Botany

233

173

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Lupines (Lupinus species; Fabaceae) are an ancient crop with great potential to be developed further for high-protein feed and food, cover crops, and phytoremediation. Being legumes, they are capable of symbiotically fixing atmospheric nitrogen. However, Lupinus species appear to be nonmycorrhizal or weakly mycorrhizal at most; instead some produce cluster roots, which release vast amounts of phosphate-mobilizing carboxylates (inorganic anions). Other lupines produce cluster-like roots, which function in a similar manner, and some release large amounts of carboxylates without specialized roots. These traits associated with nutrient acquisition make lupines ideally suited for either impoverished soils or soils with large amounts of phosphorus that is poorly available for most plants, e.g., acidic or alkaline soils. Here we explore how common the nonmycorrhizal phosphorus-acquisition strategy based on exudation of carboxylates is in the genus Lupinus, concluding it is very likely more widespread than generally acknowledged. This trait may partly account for the role of lupines as pioneers or invasive species, but also makes them suitable crop plants while we reach "peak phosphorus".

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Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

Section: Lupine Seeds For Feed and Foodmentioning

confidence: 99%

See 1 more Smart Citation

How a phosphorus‐acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae)

Lambers

Clements

Nelson

2013

American J of Botany

233

173

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“…β-Conglutin (Lup an 1) was a major allergen in patients with allergy following lupin ingestion (Sanz et al, 2010) and the major lupin allergen cross-reacted with peanut proteins, as observed in IgE-binding and SPT studies in peanut-allergic individuals (Ballabio et al, 2013). The basic subunits of the 11S globulin -conglutin may also be responsible for cross-reactivity between lupin and other leguminous plants (Ballabio et al, 2010;Sirtori et al, 2011). The high level of amino acid sequence homology between Lup-1 and Lup-2 and major allergens of some legumes explains the cross-reactivity between lupin and other legumes.…”

Section: Cross-reactivitiesmentioning

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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“…The allergenic properties of the lupin seed have been ascribed to the abundant components β- and α-conglutin [14], while for γ-conglutin the allergenic potential remains controversial, ranging from strong to weak in different in vitro and/or in vivo settings [14,15,16,17,18,19,20]. …”

Section: Introductionmentioning

confidence: 99%

In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry

et al. 2013

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The molecular characterization of bioactive food components is necessary for understanding the mechanisms of their beneficial or detrimental effects on human health. This study focused on γ-conglutin, a well-known lupin seed N-glycoprotein with health-promoting properties and controversial allergenic potential. Given the importance of N-glycosylation for the functional and structural characteristics of proteins, we studied the purified protein by a mass spectrometry-based glycoproteomic approach able to identify the structure, micro-heterogeneity and attachment site of the bound N-glycan(s), and to provide extensive coverage of the protein sequence. The peptide/N-glycopeptide mixtures generated by enzymatic digestion (with or without N-deglycosylation) were analyzed by high-resolution accurate mass liquid chromatography–multi-stage mass spectrometry. The four main micro-heterogeneous variants of the single N-glycan bound to γ-conglutin were identified as Man2(Xyl) (Fuc) GlcNAc2, Man3(Xyl) (Fuc) GlcNAc2, GlcNAcMan3(Xyl) (Fuc) GlcNAc2 and GlcNAc 2Man3(Xyl) (Fuc) GlcNAc2. These carry both core β1,2-xylose and core α1-3-fucose (well known Cross-Reactive Carbohydrate Determinants), but corresponding fucose-free variants were also identified as minor components. The N-glycan was proven to reside on Asn131, one of the two potential N-glycosylation sites. The extensive coverage of the γ-conglutin amino acid sequence suggested three alternative N-termini of the small subunit, that were later confirmed by direct-infusion Orbitrap mass spectrometry analysis of the intact subunit.

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Cross-reactivity between peanut and lupin proteins

Cited by 19 publications

References 32 publications

How a phosphorus‐acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae)

How a phosphorus‐acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae)

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

In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry

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