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glycinin/hipersensibilidad
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Inbred Chinese Wuzhishan (WZS) minipig model for soybean glycinin and beta-conglycinin allergy.
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Validated murine models have been built to assess the potential allergenicity of novel proteins. Large animals, such as pigs, share more similarities to humans in physiology and immunology than murine. Among Chinese minipigs, Wuzhishan (WZS) minipigs have the highest inbreeding coefficient, more
Oral allergy syndrome and anaphylactic reactions in BALB/c mice caused by soybean glycinin and beta-conglycinin.
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BACKGROUND
Soybean protein is used in a number of food products but is also a common cause of food allergy. Soybean glycinin and beta-conglycinin represent up to one-third of protein in the soybean. Many reports have indicated that glycinin and beta-conglycinin have been characterized as major
Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy.
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BACKGROUND
Soybean is considered an important allergenic food, but published data on soybean allergens are controversial.
OBJECTIVE
We sought to identify relevant soybean allergens and correlate the IgE-binding pattern to clinical characteristics in European patients with confirmed soy
Soybean Glycinin- and β-Conglycinin-Induced Intestinal Damage in Piglets via the p38/JNK/NF-κB Signaling Pathway.
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β-Conglycinin (7S) and glycinin (11S) are known to induce a variety of hypersensitivity reactions involving the skin, intestinal tract, and respiratory tract. The present study aimed to identify the mechanism underlying the development of allergy to soybean antigen proteins, using piglets as an
Advances of research on glycinin and β-conglycinin: a review of two major soybean allergenic proteins.
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Being an important crop, soybean is widely used in the world and plays a vital role in human and animal nutrition. However, it contains several antinutritional factors (ANFs) including soybean agglutinin, soybean protease inhibitors, soybean allergenic proteins, etc., that may result in poor food
Development and Characterization of a Soybean Experimental Line Lacking the α' Subunit of β-Conglycinin and G1, G2, and G4 Glycinin.
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A soybean experimental line (BSH-3) devoid of a subset of seed storage proteins was developed by crossing a mutant donor line "HS99B" with a Chinese cultivar "Dongnong47" (DN47). One-dimensional and high-resolution 2-D gel electrophoresis revealed the absence of G1 (A1aB2), G2 (A2B1a), and G4
Soymilk fermentation by Enterococcus faecalis VB43 leads to reduction in the immunoreactivity of allergenic proteins β-conglycinin (7S) and glycinin (11S).
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Food allergies represent a serious problem affecting human health and soy proteins rank among the most allergenic proteins from food origin. The proteolytic enzymes produced by lactic acid bacteria (LAB) can hydrolyse the major allergens present in soybean, reducing their immunoreactivity. Many
Influence of different extraction conditions on the detection of glycinin and β-conglycinin in model processed foods by ELISA
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The presence of undeclared soy proteins in food can cause severe reactions in soy allergic individuals. The extraction of target proteins from processed foods is a crucial step in allergen detection by immunoassays, as only successfully extracted target proteins can be detected by the specific
Using patient serum to epitope map soybean glycinins reveals common epitopes shared with many legumes and tree nuts.
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Soybean consumption is increasing in many Western diets; however, recent reviews suggest that the prevalence of soy allergy can be as high as 0.5% for the general population and up to 13% for children. The immunoglobulin-E (IgE) binding of sera from six soy-sensitive adult human subjects to soybean
Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3.
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BACKGROUND
The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant.
Development of immunoaffinity chromatographic method for isolating glycinin (11S) from soybean proteins.
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A monoclonal antibody (Mab), 4B2, against soybean glycinin was prepared using the preliminary extracted natural glycinin as the immunogen in our previous study. Herein, we established a novel method for the purification of glycinin by Mab 4B2-based immunoaffinity chromatography. The characteristics
Immunochemical characterization of Glycine max L. Merr. var Raiden, as a possible hypoallergenic substitute for cow's milk-allergic patients.
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BACKGROUND
Cows' milk allergy (CMA) is the most common cause of food allergy in infancy. The only proven treatment is the complete elimination of cows' milk proteins (CMPs) from the diet by means of hypoallergenic formulas. Soybean-based formulae are widely used although intolerance to soy has been
A soybean G2 glycinin allergen. 1. Identification and characterization.
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BACKGROUND
Multiple allergens have been documented in soybean extracts. IgE from individuals allergic to soybeans, but not to peanut, was shown by immunoblot analysis to bind to proteins with a molecular weight of approximately 21 kD. These findings suggested that unique proteins in soybeans might
A soybean G2 glycinin allergen. 2. Epitope mapping and three-dimensional modeling.
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BACKGROUND
Multiple allergens have been documented in soybean extracts. IgE from individuals allergic to soybeans, but not to peanut, has been shown by immunoblot analysis to bind to proteins with a molecular weight of approximately 22 kD. These findings suggested that this unique protein fraction
[Anaphylactic reactions in WZS minipig orally induced by glycinin].
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OBJECTIVE
To explore the suitable dosage and observation period of anaphylactic reactions in WZS minipigs induced by glycinin (11S).
METHODS
Twelve 45-day-old WZS minipigs were randomly divided into three groups (control group, 4% 11S group and 8% 11S group, n = 4), which were respectively orally
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