Covalent polyphenol with soybean 11S protein to develop hypoallergenic conjugates for potential immunotherapy

Li, Liuying; Chai, Wenxiang; Ma, Li; Zhang, Tingting; Chen, Jiamin; Zhang, Jian; Wu, Xuli

doi:10.1016/j.jff.2023.105518

Cited by 11 publications

(5 citation statements)

References 37 publications

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“…This results in more stable and effective polyphenol–allergen complexes [ 115 , 135 ]. Several excellent studies that examined the structural and functional characteristics of soybean globulins following covalent interaction with polyphenols such as EGCG, chlorogenic acid, caffeic acid, gallic acid, and tannic acid [ 136 , 137 , 138 ] provided clear evidence of this occurrence. There was a decrease in IgE binding activity and histamine release in vitro [ 136 , 137 , 138 ] as a consequence of structural changes caused by the formation of polyphenol–soybean globulin conjugates and the cross-linking of soybean proteins.…”

Section: Possible Modes Of Action For Treating or Preventing Allergy-...mentioning

confidence: 99%

“…These changes also increased UV absorption and protein digestibility. Curiously, studies conducted on an allergic mouse model showed that covalently conjugating the soy 11S protein with EGCG and chlorogenic acid not only reduced the protein’s allergenicity and allergy symptoms but also successfully induced oral tolerance to the soy allergen [ 138 ].…”

Section: Possible Modes Of Action For Treating or Preventing Allergy-...mentioning

confidence: 99%

See 1 more Smart Citation

Dietary Polyphenols, Plant Metabolites, and Allergic Disorders: A Comprehensive Review

Farhan,

Rizvi,

Aatif

et al. 2024

Pharmaceuticals

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Given the ongoing rise in the occurrence of allergic disorders, alterations in dietary patterns have been proposed as a possible factor contributing to the emergence and progression of these conditions. Currently, there is a significant focus on the development of dietary therapies that utilize natural compounds possessing anti-allergy properties. Dietary polyphenols and plant metabolites have been intensively researched due to their well-documented anti-inflammatory, antioxidant, and immunomodulatory characteristics, making them one of the most prominent natural bioactive chemicals. This study seeks to discuss the in-depth mechanisms by which these molecules may exert anti-allergic effects, namely through their capacity to diminish the allergenicity of proteins, modulate immune responses, and modify the composition of the gut microbiota. However, further investigation is required to fully understand these effects. This paper examines the existing evidence from experimental and clinical studies that supports the idea that different polyphenols, such as catechins, resveratrol, curcumin, quercetin, and others, can reduce allergic inflammation, relieve symptoms of food allergy, asthma, atopic dermatitis, and allergic rhinitis, and prevent the progression of the allergic immune response. In summary, dietary polyphenols and plant metabolites possess significant anti-allergic properties and can be utilized for developing both preventative and therapeutic strategies for targeting allergic conditions. The paper also discusses the constraints in investigating and broad usage of polyphenols, as well as potential avenues for future research.

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Section: Possible Modes Of Action For Treating or Preventing Allergy-...mentioning

confidence: 99%

Section: Possible Modes Of Action For Treating or Preventing Allergy-...mentioning

confidence: 99%

Dietary Polyphenols, Plant Metabolites, and Allergic Disorders: A Comprehensive Review

Farhan,

Rizvi,

Aatif

et al. 2024

Pharmaceuticals

View full text Add to dashboard Cite

show abstract

“…For example, Yan et al demonstrated that EGCG could form C–S and C–N bonds with the amino and sulfydryl groups of SPI, which improved their emulsification and antioxidant properties [2] . Similarly, Liu et al found that 11S coupled with EGCG to form crosslinked protein polymers, altering the protein structure, reducing its allergenicity, and improving its digestibility [4] . Furthermore, many studies have shown that covalent crosslinking between proteins and polyphenols results in higher binding efficiency and stability than those of the systems with non-covalent bonds [6] .…”

Section: Introductionmentioning

confidence: 97%

“…In recent years, with the increasing emphasis on healthy eating, the use of functional active compounds, such as polyphenols, for modifying proteins and developing active composite products has become a hot research topic [3] . Owing to its excellent antioxidant properties and pharmacological effects, (−)-epigallocatechin gallate (EGCG) is commonly utilized for protein modification to enhance its functional characteristics [4] . In food systems, EGCG can bind to the amino, carboxyl, and hydroxyl groups of proteins/peptides via covalent or non-covalent interactions, thereby altering their structural and functional properties [5] .…”

Section: Introductionmentioning

confidence: 99%

Ultrasound-assisted preparation of protein–polyphenol conjugates and their structural and functional characteristics

Yan,

Wang,

et al. 2023

Ultrasonics Sonochemistry

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“…Additionally, legumin is a member of the major family of proteins involved in allergens, including 2S albumin, 7S globulin, and nonspecific lipid transfer protein (nsLTP) 30 , 31 . Currently, the utilization of 11S globulin in the medical field is extensive, encompassing protein structure modification through binding with other substances to mitigate sensitization associated with 11S globulin 32 . It has previously been shown that there are two major storage proteins in soybean seeds, 7S and 11S, that affect the content and abundance of total proteins; the authors also indicated that the absence of a particular globulin polypeptide (11SA4) in their study resulted in significantly increased abundance of lectin and that the exact biological function of lectin is related to seed germination 33 .…”

Section: Introductionmentioning

confidence: 99%

Cloning and functional characterization of the legumin A gene (EuLEGA) from Eucommia ulmoides Oliver

Zheng,

Zhao

2024

Sci Rep

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Legumin A is a seed storage protein that provides nutrients for seed germination. The purpose of this study was to describe the structure and expression pattern of the EuLEGA gene in Eucommia ulmoides Oliver (E. ulmoides) and to infer its functional role. The 1287 bp coding sequence of the EuLEGA CDS of the EuLEGA gene, encoding a protein containing 428 amino acid residues, was cloned. The structure predicted that the protein belonged to the RmlC (deoxythymidine diphosphates, dTDP)-4-dehydrorhamnose 3,5-epimerase)-like cupin conserved domain family, which contains both RmlC, a key enzyme for the synthesis of rhamnose and legumin A. The overexpression (OE) vector of the EuLEGA gene was constructed and genetically transformed into tobacco and E. ulmoides; the RNA interference (RNAi) vector of the EuLEGA gene was constructed and genetically transformed into E. ulmoides; and the contents of legumin A and rhamnose were detected. The results showed that the EuLEGA gene could significantly increase the content of legumin A in transgenic tobacco leaves and transgenic E. ulmoides regenerative buds, and the OE of this gene in E. ulmoides could promote an increase in rhamnose content. RNAi caused a significant decrease in the legumin A content in the regenerated buds of E. ulmoides. These was a significant increase in legumin A in the transgenic tobacco seeds, and these results indicate that the expression of the EuLEGA gene is closely related to the accumulation of legumin A. Subcellular localization studies revealed that EuLEGA is localized to the cytoplasm with the vacuolar membrane. Analysis of the EuLEGA gene expression data revealed that the expression level of the EuLEGA gene in the samaras was significantly greater than that in the leaves and stems. In addition, the study also demonstrated that GA3 can upregulate the expression levels of the EuLEGA gene, while ABA and MeJA can downregulate its expression levels.

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Covalent polyphenol with soybean 11S protein to develop hypoallergenic conjugates for potential immunotherapy

Cited by 11 publications

References 37 publications

Dietary Polyphenols, Plant Metabolites, and Allergic Disorders: A Comprehensive Review

Dietary Polyphenols, Plant Metabolites, and Allergic Disorders: A Comprehensive Review

Ultrasound-assisted preparation of protein–polyphenol conjugates and their structural and functional characteristics

Cloning and functional characterization of the legumin A gene (EuLEGA) from Eucommia ulmoides Oliver

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