Identification of the linear immunodominant epitopes in the β subunit of β-conglycinin and preparation of epitope antibodies

Bu, Guanhao; Li, Tanghao; Zhu, Tingwei; Xi, Guanpeng

doi:10.1016/j.ijbiomac.2020.03.159

Cited by 13 publications

(18 citation statements)

References 34 publications

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“…The protein content and purity of extracted ⊎-conglycinin was 852 and 933 g kg −1 , respectively. 16 Moreover, the anti-⊎-conglycinin rabbit serum was generated by our laboratory. The epitope polyclonal antibodies (PA) were prepared following the published study.…”

Section: ⊎-Conglycinin and Antibodiesmentioning

confidence: 99%

“…The IgG and IgE binding capacities of ⊎-conglycinin were evaluated using indirect competitive enzyme-linked immunosorbent assay (ic-ELISA) described in our previous study. 16 The 100 μL of ⊎-conglycinin antigen (0.1 μg mL −1 for IgG, 20 μg mL −1 for IgE) was coated in a microtiter plate and incubated at 4 °C overnight. Meanwhile, the HHP-treated sample solution was mixed with an equivalent volume of serum.…”

Section: Igg and Ige Bindingmentioning

confidence: 99%

“…Western blotting could visually evaluate the epitope of ⊎-conglycinin after HHP treatment. 16 First, SDS-PAGE was performed to isolate the subunits of ⊎-conglycinin; the gels were then transferred to a polyvinylidene fluoride (PVDF) membrane. The membranes were blocked with 10 mol L −1 PBS containing 50 g L −1 non-fat dry milk and were incubated with antibodies.…”

Section: Western Blottingmentioning

confidence: 99%

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High hydrostatic pressure treatment reduces the potential antigenicity of β‐conglycinin by changing the protein structure during in vitro digestion

2022

J Sci Food Agric

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BACKGROUND High hydrostatic pressure (HHP) treatment has been used to alleviate the allergenicity of soybeans, but there are little data about the potential antigenicity of β‐conglycinin after HHP treatment. RESULTS We examined the effects of HHP treatment on the antigenicity and structure of β‐conglycinin. When the pressure was 300 and 400 MPa, HHP treatment reduced the immunoglobulin (Ig)G binding capacity of β‐conglycinin, while its IgE binding capacity did not change significantly. After in vitro digestion, both the IgE and IgG binding of β‐conglycinin was obviously inhibited after HHP treatment at 400 MPa and 60 °C, although its binding capacity with linear epitope antibodies increased. Moreover, HHP treatment changed the secondary structure of β‐conglycinin, the content of α‐helix and random coils increased, while the β‐sheet and β‐turn decreased. After HHP treatment, the conformational structure was unfolded so that a large number of hydrophobic regions were exposed. CONCLUSION HHP treatment alleviated the potential antigenicity of β‐conglycinin by modifying its structure, which facilitated in vitro digestion and destroyed epitopes. This research provides a new insight into the mechanism of HHP treatment that affects the sensitization of soy protein allergens. © 2022 Society of Chemical Industry.

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Section: ⊎-Conglycinin and Antibodiesmentioning

confidence: 99%

Section: Igg and Ige Bindingmentioning

confidence: 99%

Section: Western Blottingmentioning

confidence: 99%

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High hydrostatic pressure treatment reduces the potential antigenicity of β‐conglycinin by changing the protein structure during in vitro digestion

2022

J Sci Food Agric

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“…So far, 390 proteins have been identified as food protein allergens by the World Health Organization and the International Union of Immunological Societies (WHO/IUIS) Allergen Nomenclature Sub-Committee, and more than 50% of the food protein allergens are found in eggs, milk, nuts, wheat, crustaceans, beans, fish, and peanuts [2]. Soybean is a common source for legume allergen, and about 25% of food allergies are caused by soybeans [3,4], which not only induce a variety of pathological reactions such as intestinal injury, stomach discomfort, or allergic dermatitis, anaphylactic shock, [3], but also limit the development and application of soybean products [4]. So far, eight soybean protein allergens have been identified and submitted to the allergen database (http://www.allergen.org/), namely hydrophobic protein (Gly m 1), defensin (Gly m 2), profilin (Gly m 3), pathogenesis-related protein (Gly m 4), β-conglycinin (Gly m 5), glycinin (Gly m 6), seed biotinylated protein (Gly m 7) and 2S albumin ( Gly m 8).…”

Section: Introductionmentioning

confidence: 99%

Prediction and characterization of the T cell epitopes for the major soybean protein allergens using bioinformatics approaches

Zhou

Wang

et al. 2021

Preprint

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Protein allergens is a health risk for consumption of soybeans. To understand allerginicity mechanism, T cell epitopes of 7 soybean allergens were predicted and screened by abilities to induce cytokine interleukin 4. The relationships among amino acid composition, properties, allergenicity and pepsin hydrolysis sites were analyzed. Among the 138 T cell epitopes identified, YIKDVFRVIPSEVLS, KDVFRVIPSEVLSNS, DVFRVIPSEVLSNSY of Gly m 6.0501 (P04347), and AKADALFKAIEAYLL, ADALFKAIEAYLLAH of Gly m 4.0101 (P26987) were the most possible epitope candidates. In T cell epitopes pattern, the frequencies of amino acids Q, D, E, P and G decreased, while F, I, N, V, K and H increased. Hydrophobic residues at positions p1 and p2 and positively charged residues in positions p13 might contribute to allergenicity. Most of epitopes could be hydrolyzed by pepsin into small polypeptides within 12 residues length, and the anti-digestive epitope regions contained I, V, S, N, and Q residues. T cell epitopes EEQRQQEGVIVELSK from Gly m 5.03 (P25974) showed resistantence to pepsin hydrolysis and would cause a higher Th2 cell response. This research provides basis for the development of hypoallergenic soybean products in the soybean industry as well as for the immunotherapy design for protein allergy.

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“…So far, 390 proteins have been identified as food protein allergens by the World Health Organization and the International Union of Immunological Societies (WHO/IUIS) Allergen Nomenclature Sub‐Committee, and more than 50% of the food protein allergens belong to eggs, milk, nuts, wheat, crustaceans, beans, fish, and peanuts 2 . Soybean is a common source for legume allergen, and about 25% of food allergies are caused by soybeans, 3,4 not only will induce a variety of pathological reactions such as intestinal injury, stomach discomfort, or allergic dermatitis, anaphylactic shock,, 3 but also limit the development and application of soybean products 4 . So far, eight soybean protein allergens have been identified and submitted to the allergen database (http://www.allergen.org/), namely hydrophobic protein (Gly m 1), defensin (Gly m 2), profilin (Gly m 3), pathogenesis‐related protein (Gly m 4), β‐conglycinin (Gly m 5), glycinin (Gly m 6), seed biotinylated protein (Gly m 7) and 2S albumin (Gly m 8).…”

Section: Introductionmentioning

confidence: 99%

Prediction and characterization of the T cell epitopes for the major soybean protein allergens using bioinformatics approaches

Zhou

Wang

et al. 2021

Proteins

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Protein allergens is a health risk for consumption of soybeans. To understand allerginicity mechanism, T cell epitopes of 7 soybean allergens were predicted and screened by abilities to induce cytokine interleukin (IL) 4. The relationships among amino acid composition, properties, allergenicity, and pepsin hydrolysis sites were analyzed. Among the 138 T cell epitopes identified, YIKDVFRVIPSEVLS, KDVFRVIPSEVLSNS, DVFRVIPSEVLSNSY of Gly m 6.0501 (P04347), and AKADALFKAIEAYLL, ADALFKAIEAYLLAH of Gly m 4.0101 (P26987) were the most possible epitope candidates. In T cell epitopes pattern, the frequencies of amino acids Q, D, E, P, and G decreased, while F, I, N, V, K, H, A, L, and S increased. Hydrophobic residues at positions p1 and p2 and positively charged residues in positions p13 might contribute to allergenicity. Most of epitopes could be hydrolyzed by pepsin into small polypeptides within 12 residues length, and the anti-digestive epitope regions contained I, V, S, N, and Q residues. T cell epitopes EEQRQQEGVIVELSK from Gly m 5.03 (P25974) showed resistance to pepsin hydrolysis and would cause a higher Th2 cell response. This research provides basis for the development of hypoallergenic soybean products in the soybean industry as well as for the immunotherapy design for protein allergy.

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Identification of the linear immunodominant epitopes in the β subunit of β-conglycinin and preparation of epitope antibodies

Cited by 13 publications

References 34 publications

High hydrostatic pressure treatment reduces the potential antigenicity of β‐conglycinin by changing the protein structure during in vitro digestion

High hydrostatic pressure treatment reduces the potential antigenicity of β‐conglycinin by changing the protein structure during in vitro digestion

Prediction and characterization of the T cell epitopes for the major soybean protein allergens using bioinformatics approaches

Prediction and characterization of the T cell epitopes for the major soybean protein allergens using bioinformatics approaches

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