Legume Protein Consumption and the Prevalence of Legume Sensitization

Smits, Mark; Le, Thuy My; Welsing, Paco; Houben, Geert F.; Knulst, André C.; Verhoeckx, Kitty

doi:10.3390/nu10101545

Cited by 22 publications

(20 citation statements)

References 59 publications

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“…Lupine has been ranked ninth in the category of "risk allergens" [2] while soybean is one of the eight groups of foods accountable for about 90% of food-allergic reactions [1,3]. Among sensitized children, 6% were diagnosed with soybean allergy while an overall prevalence of 2.1% was found in a study involving several European countries, the USA, and Australia [1,4,5]. Regarding lupine allergy, the prevalence varies, depending on dietary habits and geographical differences [1,6].…”

Section: Introductionmentioning

confidence: 99%

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Villa

Moura

Costa

2020

Foods

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Lupine and soybean are important technological aids for the food industry. However, they are also capable of inducing severe allergic reactions in food-sensitized/allergic individuals. In this context, this work intended to study the combined effects of thermal processing and food matrix on the immunoreactivity of lupine and soybean proteins used as ingredients in bakery and meat products, respectively. For this purpose, the effects of baking, mild oven cooking, and autoclaving on the protein profiles were evaluated, using model mixtures simulating the production of lupine-containing breads and soybean-containing cooked hams/sausages, by native- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and immunoblotting using specific antibodies. The results showed that lupine gamma-conglutin immunoreactivity was slightly decreased in wheat flour mixtures compared to rice, but it was more pronounced in baked products. In meat mixtures, substantial protein fragmentation was noted after autoclaving, with decreased immunoreactivity of soybean trypsin inhibitor. The analysis of 22 commercial products enabled the identification of lupine gamma-conglutin in four bakery samples and soybean trypsin-inhibitor in five sausages, and further differentiated autoclaved from other milder thermally treated products. Generally, the immunoreactivity of target proteins was reduced by all the tested thermal treatments, though at a higher extent after autoclaving, being slightly altered by the food matrix.

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Section: Introductionmentioning

confidence: 99%

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Villa

Moura

Costa

2020

Foods

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“…No inhibition could be observed in pea-allergic patient 12 and in pea-tolerant patient 17. rPis s 1 was able to inhibit IgE binding in the lower molecular weight (LMW) range ( Figure 1A, patient nos. 3,4,11,14) where mass spectrometry confirmed the presence of PA1 isoforms and PA2 ( Figure S2, Table S2b). In addition, PA1 was confirmed as 11 kDa full-length proprotein instead of 6 and 4 kDa proteolytic fragments (data not shown).…”

Section: High Ige Binding Capacity Of Pis S 1 Compared To Pea Totalmentioning

confidence: 90%

“…28 Briefly, RBL-2H3 cells expressing the α-chain of the human IgE receptor FcεRI were sensitized overnight with a 1:10 diluted serum pool of pea-allergic patients (nos. 1,3,4,8,11). Cells were stimulated with serial dilutions of either rPis s 1, pea extract or BSA as negative control.…”

Section: Mediator Release From Humanized Rat Basophilic Leukaemia (mentioning

confidence: 99%

“…To further address the relevance of Pis s 1 in this study population, the IgE inhibition capacity of rPis s 1 against pea total protein extract was determined densitometrically on immunoblots ( Figure 1A, Table 1 1,2,4,8,9) and one pea-tolerant child (16) partially. No inhibition could be observed in pea-allergic patient 12 and in pea-tolerant patient 17. rPis s 1 was able to inhibit IgE binding in the lower molecular weight (LMW) range ( Figure 1A, patient nos.…”

Section: High Ige Binding Capacity Of Pis S 1 Compared To Pea Totalmentioning

confidence: 99%

“…2,3 Food allergy to legumes, such as peanut, soya bean and lupin, has been well documented, as was recently summarized. 4,5 In foods, the use of these allergenic legumes as ingredients requires mandatory labelling in the EU, in order to enable allergic consumers to immediately identify and avoid these allergens. 6 In addition, peanut and soya bean allergens have been characterized extensively on the molecular level.…”

Section: Introductionmentioning

confidence: 99%

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Pea (Pisum sativum) allergy in children: Pis s 1 is an immunodominant major pea allergen and presents IgE binding sites with potential diagnostic value

Popp

Trendelenburg

Niggemann

et al. 2020

Clin Experimental Allergy

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Background: Food allergy to pea (Pisum sativum) has been rarely studied in children at the clinical and molecular levels.Objective: To elucidate the allergenic relevance and diagnostic value of pea 7S globulin Pis s 1, nsLTP, and 2S albumins PA1 and PA2 in children. Methods:Children with pea-specific IgE ≥ 0.35 kU A /L and clinical evidence of pea allergy or tolerance were included in the study. IgE binding against pea total protein extract, recombinant (r) rPis s 1, rPA1, rPA2, and natural nsLTP was analysed using IgE immunoblot/inhibition. Mediator release potency was investigated in passively sensitized rat basophil leukaemia (RBL) 2H3-cells. IgE binding to synthetic overlapping peptides of Pis s 1 was detected on multipeptide microarrays.Results: 19 pea-sensitized children were included, 14 with doctors' diagnosed allergy and 5 with tolerance to pea (median age 3.5 and 4.5 years, respectively). 11/14 (78%) pea-allergic and 1/5 (20%) tolerant children were sensitized to Pis s 1. Under the reducing conditions of immunoblot analysis, IgE binding to rPA1 was negligible, sensitization to rPA2 and nsLTP undetectable. Compared to pea total protein extract, rPis s 1 displayed on average 58% IgE binding capacity and a 20-fold higher mediator release potency. Selected Pis s 1-related peptides displayed IgE binding in peaallergic but not in pea-tolerant children. Conclusions and Clinical Relevance:In this study group, Pis s 1 is a major immunodominant allergen in pea-allergic children. Evidence for sensitization to nsLTP and 2S albumins was low but requires further verification with regard to conformational epitopes. Recombinant Pis s 1 and related peptides which were exclusively recognized by pea-allergic children may improve in vitro diagnosis of pea allergy once verified in prospective studies with larger study groups. K E Y W O R D S2S albumin, diagnosis, epitopes, IgE, lipid-transfer protein, pea allergy, Pis s 1, vicilinThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Prospects for developing allergen‐depleted food crops

Lokya,

Parmar,

Pandey

et al. 2023

The Plant Genome

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In addition to the challenge of meeting global demand for food production, there are increasing concerns about food safety and the need to protect consumer health from the negative effects of foodborne allergies. Certain bio‐molecules (usually proteins) present in food can act as allergens that trigger unusual immunological reactions, with potentially life‐threatening consequences. The relentless working lifestyles of the modern era often incorporate poor eating habits that include readymade prepackaged and processed foods, which contain additives such as peanuts, tree nuts, wheat, and soy‐based products, rather than traditional home cooking. Of the predominant allergenic foods (soybean, wheat, fish, peanut, shellfish, tree nuts, eggs, and milk), peanuts (Arachis hypogaea) are the best characterized source of allergens, followed by tree nuts (Juglans regia, Prunus amygdalus, Corylus avellana, Carya illinoinensis, Anacardium occidentale, Pistacia vera, Bertholletia excels), wheat (Triticum aestivum), soybeans (Glycine max), and kidney beans (Phaseolus vulgaris). The prevalence of food allergies has risen significantly in recent years including chance of accidental exposure to such foods. In contrast, the standards of detection, diagnosis, and cure have not kept pace and unfortunately are often suboptimal. In this review, we mainly focus on the prevalence of allergies associated with peanut, tree nuts, wheat, soybean, and kidney bean, highlighting their physiological properties and functions as well as considering research directions for tailoring allergen gene expression. In particular, we discuss how recent advances in molecular breeding, genetic engineering, and genome editing can be used to develop potential low allergen food crops that protect consumer health.

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Legume Protein Consumption and the Prevalence of Legume Sensitization

Cited by 22 publications

References 59 publications

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Pea (Pisum sativum) allergy in children: Pis s 1 is an immunodominant major pea allergen and presents IgE binding sites with potential diagnostic value

Prospects for developing allergen‐depleted food crops

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