Purification and IgE-binding properties of soybean β-conglycinin subunits

Zheng, Suiping; Tian, He; Ma, Na; Sun, Zewei; Yu, Chunyan

doi:10.1016/j.procbio.2012.07.003

Cited by 13 publications

(6 citation statements)

References 41 publications

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“…Four of the six identified proteins in this study have been described as human food allergens including maize/potato GBSS‐1, soybean glycinin (Gly m 6), soybean β‐conglycinin (Gly m 5), and potato aspartic protease inhibitor (Sol t 2) . These proteins have been defined as allergens by their IgE‐binding properties.…”

Section: Discussionmentioning

confidence: 94%

“…These proteins have been defined as allergens by their IgE‐binding properties. In a few cases, proteins were defined as allergens based on their capacity to induce histamine release from basophils, to trigger a positive skin test, or to reduce allergenicity of the food when the allergen is not expressed . Interestingly, soybean β‐conglycinin has also been described as an allergen in animals, including dogs, with the β chain being an important antigen across species .…”

Section: Discussionmentioning

confidence: 99%

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Detection of IgE‐reactive proteins in hydrolysed dog foods

Roitel¹,

Bonnard²,

Stella

et al. 2017

Veterinary Dermatology

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Detection of IgE‐reactive proteins in hydrolysed dog foods

Roitel¹,

Bonnard²,

Stella

et al. 2017

Veterinary Dermatology

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“…Firstly, crude β-conglycinin was extracted from soybean seeds by the method of Zheng et al with some modifications [9]. Its three subunits were isolated using SDS-PAGE.…”

Section: Methodsmentioning

confidence: 99%

“…The percentage of each subunit varies among genotypes: α from 10.4% to 20.8%, α’ from 8.1% to 20.7% and β from 4.5% to 12.9% of total proteins [6,7]. All three subunits have been purified and tested to have allergenic activity [8,9]. Since the antigenic IgG-binding epitopes (S185-R231) have been identified near the N terminus of the α-subunit [10], the allergenic activity of the α subunit is highest among them [11].…”

Section: Introductionmentioning

confidence: 99%

“…Recently, immunoassays, such as IgE-immunoblotting and enzyme-linked immunosorbent assays (ELISA), have been the common approach for identification and quantification of soy allergens. For example, ELISA with polyclonal antibodies have been used to detect α subunit of β-conglycinin [9,11,16]. However, the immunoassays may suffer from other limitations such as antibody availability and high variability, and low sensitivity and specificity, especially among allergen protein families.…”

Section: Introductionmentioning

confidence: 99%

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Quantification of Gly m 5.0101 in Soybean and Soy Products by Liquid Chromatography-Tandem Mass Spectrometry

et al. 2018

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Gly m 5.0101, the alpha subunit of β-conglycinin, is one of the major allergens found in soybeans that has been identified as causing an allergic reaction. Here, we developed a quantification method of Gly m 5.0101 with multiple reaction monitoring using the synthetic peptide 194NPFLFGSNR202 as the external standard. Firstly, the ground soybean was defatted and extracted with a protein extraction buffer. Then the crude extract was on-filter digested by trypsin and analyzed by liquid chromatography-tandem mass spectrometry. The selected peptide exhibited a detection limit of 0.48 ng/mL and a linear relationship in a concentration range from 1.6 to 500 ng/mL (r2 > 0.99). The developed method was successfully applied to quantify the Gly m 5.0101 level in dozens of soybean varieties from different sources and soybean products derived from different processing techniques. The developed method could be used to further analyze β-conglycinin in soybean seeds combined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.

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Legume Allergens Pea, Chickpea, Lentil, Lupine and Beyond

Abu Risha,

Rick,

Plum

et al. 2024

Curr Allergy Asthma Rep

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Purpose of the Review In the last decade, an increasing trend towards a supposedly healthier vegan diet could be observed. However, recently, more cases of allergic reactions to plants and plant-based products such as meat-substitution products, which are often prepared with legumes, were reported. Here, we provide the current knowledge on legume allergen sources and the respective single allergens. We answer the question of which legumes beside the well-known food allergen sources peanut and soybean should be considered for diagnostic and therapeutic measures. Recent Findings These “non-priority” legumes, including beans, pea, lentils, chickpea, lupine, cowpea, pigeon pea, and fenugreek, are potentially new important allergen sources, causing mild-to-severe allergic reactions. Severe reactions have been described particularly for peas and lupine. An interesting aspect is the connection between anaphylactic reactions and exercise (food-dependent exercise-induced anaphylaxis), which has only recently been highlighted for legumes such as soybean, lentils and chickpea. Most allergic reactions derive from IgE cross-reactions to homologous proteins, for example between peanut and lupine, which is of particular importance for peanut-allergic individuals ignorant to these cross-reactions. Summary From our findings we conclude that there is a need for large-scale studies that are geographically distinctive because most studies are case reports, and geographic differences of allergic diseases towards these legumes have already been discovered for well-known “Big 9” allergen sources such as peanut and soybean. Furthermore, the review illustrates the need for a better molecular diagnostic for these emerging non-priority allergen sources to evaluate IgE cross-reactivities to known allergens and identify true allergic reactions.

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Purification and IgE-binding properties of soybean β-conglycinin subunits

Cited by 13 publications

References 41 publications

Detection of IgE‐reactive proteins in hydrolysed dog foods

Detection of IgE‐reactive proteins in hydrolysed dog foods

Quantification of Gly m 5.0101 in Soybean and Soy Products by Liquid Chromatography-Tandem Mass Spectrometry

Legume Allergens Pea, Chickpea, Lentil, Lupine and Beyond

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