Lupine allergen detecting capability and cross-reactivity of related legumes by ELISA

Koeberl, Martina; Sharp, Michael F.; Tian, Rongkai; Buddhadasa, Saman; Clarke, Dean; Roberts, James H.

doi:10.1016/j.foodchem.2018.02.043

Cited by 31 publications

(20 citation statements)

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“…However, they exhibited main disadvantages in comparison to the current study: The protein extraction protocol in the current study is highly specific for the extraction of the vicilin family of proteins (β-conglutins), based on the presence of NaCl (0.25M) in the extraction buffer [33]. Previous studies made protein extractions using general protein extraction buffers [4,45,47], or using alternative methods from commercial kits [48] currently no longer available (Abnova, ), displaying very limited or no information about: (i) The antibody design; (ii) antibody production and use in the ELISA detection method; (iii) the limited information about protocol for total proteins extraction, which may not be specific for β-conglutin extraction; (iv) no information about lupin species used [46,48] to obtain this protein extract. The last two are the main factors with high impact in the protein extract characteristics, such as a low amount or not of Lup an 1 content.…”

Section: Resultsmentioning

confidence: 99%

“…In comparison, other ELISA methods previously developed showed low specificity of their antibodies used in the ELISA methods, since cross-reactivity showed with other legumes: Either with pea, chickpea, peanut, lentil, and soy [45], with brown bean and fenugreek (Holden et al, 2007); black bean and soy [46]; or even with non-legume proteins such as sunflower seed, cashew, almond, and pumpkin seed [61]. Furthermore, Koeberl et al [48] used three available commercial kits to analyze cross-reactivity between lupin and other legume proteins finding that all peanut samples tested showed cross-reactivity on ELISA test kit B and C [48]. In addition, cross-reactivity was also described for the entire lentil samples analyzed, thus promoting false positive results in all analyzed legume samples.…”

Section: Resultsmentioning

confidence: 99%

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Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods

Lima-Cabello

Alché

Jiménez-López

2019

Foods

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The increasing prevalence of lupin allergy as a consequence to the functional characteristics of a growing number of sweet lupin-derived foods consumption makes the imperious necessity to develop analytical tools for the detection of allergen proteins in foodstuffs. The current study developed a new highly specific, sensitive and accurate ELISA method to detect, identify and quantify the lupin main allergen β-conglutin (Lup an 1) protein in natural and processed food. The implementation of accurate standards made with recombinant conglutin β1, and an anti-Lup an 1 antibody made from a synthetic peptide commonly shared among β-conglutin isoforms from sweet lupin species was able to detect up to 8.1250 ± 0.1701 ng (0.0406 ± 0.0009 ppm) of Lup an 1. This identified even lupin traces present in food samples which might elicit allergic reactions in sensitized consumers, such as β-conglutin proteins detection and quantification in processed (roasted, fermented, boiled, cooked, pickled, toasted, pasteurized) food, while avoiding cross-reactivity (false positive) with other legumes as peanut, chickpea, lentils, faba bean, and cereals. This study demonstrated that this new ELISA method constitutes a highly sensitive and reliable molecular tool able to detect, identify and quantify Lup an 1. This contributes to a more efficient management of allergens by the food industry, the regulatory agencies and clinicians, thus helping to keep the health safety of the consumers.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods

Lima-Cabello

Alché

Jiménez-López

2019

Foods

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“…Until recently, lupine has not been widely available in Canada, but will likely become more popular because of its purported health benefits [ 8 ]. Therefore, more education about lupine is necessary for peanut-allergic Canadians and those who prepare foods for peanut-allergic individuals.…”

Section: Discussionmentioning

confidence: 99%

First reported case in Canada of anaphylaxis to lupine in a child with peanut allergy

Soller

Vieille

Chan

2018

Allergy Asthma Clin Immunol

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BackgroundLupine is a member of the legume family and is often used in many food products in Europe (e.g. pasta, pizza, sauces, etc.) as a wheat or soy substitute. Lupine cross-reacts with peanut, and cases of allergic reactions to lupine in peanut-allergic patients have been reported in Europe mainly. In contrast, lupine as an ingredient in food products is relatively new to the Canadian market.Case presentationWe describe a 10-year old boy with diagnosed peanut and tree-nut allergy, who developed anaphylaxis to lupine flour in May 2017. A few minutes after eating a pre-made pancake mix that didn’t contain any of his known allergens (peanuts, tree nuts), he developed oral pruritis followed by throat tightness, severe stomach ache, lightheadedness, cough, hoarse throat, nasal congestion, sneezing, and fatigue. He refused epinephrine, but was given cetirizine. The symptoms resolved after 3 h, but he was still unwell the following day. In a conversation between the mother and the allergist, it was determined that lupine was likely the cause of the reaction. To confirm, he was brought into clinic for skin testing to lupine. Results were consistent with lupine allergy (pancake mix: 10 × 7 mm, lupine bean: 12 × 6 mm). The family has since reported this to the Canadian Food Inspection Agency, resulting in a product recall and a consumer advisory bulletin published by Health Canada.ConclusionsThis is the first reported case of allergic reaction to lupine in Canada, and highlights the need for education of Canadian families with peanut allergy as well as allergists, regarding the possibility of cross-reactivity between peanut and lupine and its new presence in the Canadian food supply. In addition, a precautionary label for those with peanut allergy who purchase products containing lupine should be considered. This case illustrates also the need for a clear mechanism for consumers and allergists to report emerging food allergens to regulatory bodies such as Health Canada.Electronic supplementary materialThe online version of this article (10.1186/s13223-018-0303-4) contains supplementary material, which is available to authorized users.

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“…Owing to the increasing demand for specific allergen detection, a wide range of commercial kits for lupine detection has become available in the market and summarized in Table 5. Moreover, in‐house developed‐systems are frequently reported in the literature (Table 4) (Ecker & Cichna‐Markl, 2012; Ecker, Ertl, Pulverer, et al., 2013; Ecker, Ertl, & Cichna‐Markl, 2013; Holden, Faeste, & Egaas, 2005; Holden, Moen, Sletten, & Dooper, 2007; Kaw, Hefle, & Taylor, 2008; Koeberl et al., 2018; Lima‐Cabello, Alché, & Jimenez‐Lopez, 2019; Revák, Golian, Židek, Capla, & Zajác, 2014; Röder, Kleiner, Sachs, Keil, & Holzhauser, 2013). The majority of these systems relies on polyclonal antibodies (IgY from hen's eggs or IgG from rabbit) targeting lupine proteins from one or more Lupinus spp., normally providing suitable specificity for all the sweet lupine species used as food ingredients or technological aids.…”

Section: Analytical Methods For Lupine Detection In Foodsmentioning

confidence: 99%

“…The comparison of different ELISA kits from distinct manufacturers is quite difficult because each one has their own generated antibodies, conjugates, standards, and calibrants (Table 5). Koeberl et al (2018) performed an interesting comparison of three different ELISA kits to detect lupine protein or lupine flour protein from one or more species, realizing that the specificity of the antibodies used in the kits was not available, which is an important information for the detection capability to lupine and cross-reactivity phenomena. The estimated concentration of lupine in foods differed among the kits due to the use of different standards and crossreactivity was observed with some legumes and nuts.…”

Section: Immunochemical Assaysmentioning

confidence: 99%

Lupine allergens: Clinical relevance, molecular characterization, cross‐reactivity, and detection strategies

Villa

Costa

2020

Comp Rev Food Sci Food Safe

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Lupine is commonly utilized as a technological food and ingredient in a great variety of processed products (snacks, bakery, meat, and dairy products) principally owing to its nutritional value and technological properties. However, its ingestion, even at trace amounts (in the range of mg protein per kg of food), can lead to severe adverse reactions in allergic individuals. Lupine belongs to the Leguminosae family, having the conglutins (α-, β-, δ-, and γ-) as allergens, among other proteins. Cross-sensitization of lupine-sensitized individuals with other legume species, mainly peanut, can occur, but the associated clinical reactivity is still unclear. The protection of the sensitized individuals should depend on an avoidance diet, which should rely on the compliance of food labeling and, as such, on their verification by analytical methods. Food processing, such as heat treatments, has an important influence on the structural properties of lupine proteins, altering their detectability and allergenicity. In this review, different aspects related with lupine allergy are described, namely, the overall prevalence, clinical relevance, diagnosis, and treatment. The characterization of lupine allergens and their potential cross-reactivity with other legumes are critically discussed. The effects of food matrix, processing, and digestibility on lupine proteins, as well as the available analytical tools for detecting lupine at trace levels in foods, are also herein emphasized. K E Y W O R D S allergen, analytical methods, food allergy, Lupinus species, protein 1 INTRODUCTION Lupine belongs to the Lupinus genus from the Fabaceae or Leguminosae family, which also comprises soybean, peanut, chickpea, and other types of legumes (Villarino, Jayasena, Coorey, Chakrabarti-Bell, & Johnson, 2016). From approximately 450 known species of lupine, four are of agricultural and commercial interest: Lupinus albus (white lupine), native from the Mediterranean region and Africa; Lupinus angustifolius (blue lupine) from Australia; Lupinus luteus (yellow lupine) from Central Europe; and Lupinus mutabilis from South America (Jappe & Vieths, 2010; Sanz, de Las Marinas, Fernandez, & Gamboa, 2010). According to FAOSTAT, a total world production of 1,188,213 tonnes of lupine was reached in 2018. Australia is the main producer, with 714,254 tonnes in 2018, accounting to 60.1% of total world lupine production. In Europe, Russia and Poland are the main producers, reaching 136,352 and 124,314 tonnes in 2018, respectively, corresponding to 39.9% and 36.4% of total lupine production in Europe, respectively (FAOSTAT [http://www.fao.org/ faostat/en/#home]).

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Lupine allergen detecting capability and cross-reactivity of related legumes by ELISA

Cited by 31 publications

References 30 publications

Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods

Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods

First reported case in Canada of anaphylaxis to lupine in a child with peanut allergy

Lupine allergens: Clinical relevance, molecular characterization, cross‐reactivity, and detection strategies

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