MICROCHEMICAL JOURNAL
·
2024
·
IF 4.9
Jinru Zhou,Yanbo Wang,Lei Zheng,Huan Li
Seafood allergy represents a critical public health challenge, necessitating the implementation of sensitive, precise, and quantitative detection methods for seafood allergens to guarantee accurate food labeling. Parvalbumin (PV) and tropomyosin (TM) are recognized as the primary allergens in fish and shellfish. Herein, we designed a fluorescence sensing system for the simultaneous detection of PV and TM that employs aptamer-initiated catalytic hairpin assembly (CHA). In this strategy, we utilized four hairpin dimers (H1, H2, H3, and H4) as foundational elements to create the sensing scaffolds. The CHA-based fluorescent aptasensor demonstrated an extensive linear range, ranging from 0.001 μg/mL to 100 μg/mL, with detection limits of 0.29 μg/mL for PV and 0.27 μg/mL for TM. This biosensor demonstrates exceptional selectivity and stability, in addition to good accuracy. Importantly, this biosensor has been effectively utilized to quantify PV and TM in four different commercial food products, achieving satisfactory accuracy. With these advantages, our proposed CHA-based aptasensor can offer a universal tool for sensitive and precise detection of food allergens in commercial foods throughout the supply chain.
研究领域:
生物化学
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食品安全检测
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分子诊断
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DOI
高影响因子
Frontiers in Nutrition
·
2025
·
IF 5.1
Yanchu Li,Yuying Yang,Junyao Li,Rui Guo,Zhiqiang Niu,Weicheng Hu,Shucheng Liu,Shuai Wei
Introduction: Tropomyosin (TM) is the primary allergen in Litopenaeus vannamei, which usually causes allergic reactions that may be health or even life-threatening for consumers. Therefore, exploring the sensitization mechanism is of great significance for the prevention and treatment of tropomyosin allergy.Methods and results: In this study, TM sensitization models were using Balb/c mice, Caco-2 cells and RBL-2H3 cells to reveal the sensitization effect. The results of ELISA and RT-qPCR showed that TM can exacerbate the allergic reaction by reducing the mRNA expression of tight junction (TJ) proteins (such as ZO-1, claudin-3, Occludin) in the jejunum, destroying the intestinal barrier function, increasing the permeability, and promoting the release of inflammatory factors (such as IL-8, TNF-α) and histamine. The pathological results of intestinal tissue sections showed that TM also caused an increase in intestinal inflammatory infiltration in mice. RNA-seq analysis revealed that key genes (CCL2, HSP1A, GM-CSF, etc.) and PI3K/Akt signaling pathway were involved in the sensitization process. In vitro experiments were conducted to construct TM sensitized Caco-2 and RBL-2H3 cell models at a dose of 100 mg/mL. The results indicated that TM upregulated the expression of phosphorylated PI3K/ Akt and NFκB pathways in Caco-2 cells, further damaged the TJ structure of intestinal epithelial cells and promoted the release of inflammatory factors. The RBL-2H3 cell degranulation assay indicated that TM could directly stimulate the release of TNF-α from mast cells.Conclusion: The above experimental results indicated that PI3K/Akt signaling pathways play a crucial role in the induction of TM allergic responses, which provides a theoretical basis for the occurrence, development and prevention of TM allergy.
研究领域:
免疫学
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分子生物学
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药理学
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生物医学
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Xiangfei Hu,Hui Wang,Yueming Hu,Pingwei Wen,Xiongchen Wu,Zongcai Tu
The effect of electric field intensities (EFIs, 5–20 kV/cm) and treatment times (0.5–2 h) on allergenicity and spatial conformation of prawn tropomyosin was evaluated. The results demonstrated that the IgG and IgE binding capacity of tropomyosin maximally increased by 24.34 % and 29.16 % respectively, followed by a subsequent decrease after 20 kV/cm treatment for 1 h. Interestingly, 5–10 kV/cm treatments significantly decreased the α-helix content ( P < 0.05) and fluorescence intensity, while 20 kV/cm treatment promoted extensive spiralization, resulting in a tightly packed structure. The increased flexibility further exposed the hydrolysis sites and strengthened the gastrointestinal digestibility of tropomyosin. Additionally, molecular dynamic simulation indicated that extended EFIs increased structural flexibility and depolymerized the tropomyosin dimers through destroying intermolecular hydrogen bonds (formed within arginine and glutamate), which allowed tropomyosin to be easily recognized by IgG/IgE. Whereas, decrease of solvent-accessibility surface area (SASA), hydrophobic surface area induced conformation folded and caused epitopes masked.
研究领域:
食品科学
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过敏研究
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生物物理
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分子生物学
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2026
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IF 10.4
Chundi Yu,Ying Zhang,Zekun Ma,Ishfaq Ahmed,Tianjiao Xu,Qingli Yang,Liangtao Lv
Tropomyosin (TM), a major shrimp allergen, poses a significant challenge to food safety. This study aimed to develop a biosynthetic recombinant tropomyosin (rTM) as a standardized alternative to the natural tropomyosin (nTM) and to establish a sensitive detection method. Structural analyses using ultraviolet, fluorescence, and circular dichroism spectroscopies confirmed high similarity between rTM and nTM. Comparable allergenicity was further validated in a murine model. A novel lateral flow immunoassay (LFIA) employing Prussian blue nanoparticles (PBNPs) as probes was subsequently developed. This assay exhibited a wide linear range of 0.1–50 μg/mL and a low detection limit of 0.051 μg/mL, and excellent specificity, accuracy, and precision in spiked food matrices. This work establishes a foundation for developing nTM alternatives and provides a reliable, portable platform for sensitively detecting macromolecular food allergens.
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产品关联
DOI
PubMed
高影响因子
FOOD CONTROL
·
2022
·
IF 6.652
Jinru Zhou,Yanbo Wang,Chaosheng Zhou,Lei Zheng,Linglin Fu
Shellfish allergy represents a crucial public health problem, resulting in an urgent requirement for an accurate, simple, and reliable method to quantify shellfish allergens in the complex food system. Tropomyosin (TM) is known as the major allergen in shellfish. Herein, a novel switch-conversional ratiometric fluorescent biosensor, using TM-specific aptamer as the recognition probe, was developed to detect TM in the complex food system. The proposed aptasensor exhibited good accuracy, stability, and selectivity for the quantification of TM in foodstuffs. Furthermore, the applicability of this proposed aptasensor in complex food samples was verified using seven different shellfish samples. Therefore, this ratiometric fluorescent aptasensor enables accurately detecting the presence of TM traces in foods, providing technical support for allergen label supervision.
研究领域:
食品科学
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分析化学
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生物技术
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过敏与免疫学
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DOI
高影响因子
Food Analytical Methods
·
2022
·Vol. 15
·期 6
·1535-1544
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IF 3.498
Li Linfang,Zhou Jinru,Wang Kuiwu,Chen Xiaojing,Fu Linglin,Wang Yanbo
Tropomyosin (TM), known as the major allergen in shellfish, has gained increasing concerns in industrialized countries, resulting in an urgent need for an accurate, simple, and sensitive method for TM detection in food products. Nucleic acid aptamers, short single-stranded oligonucleotides chains, can bind to various targets with a high affinity and specificity and hence have the potential to be used for the accurate detection of targets. Here, we proposed capillary electrophoresis-systematic evolution of ligands by exponential enrichment (CE-SELEX) for rapid selection and identification of specific aptamers against shellfish TM. A selected aptamer IX exhibited high specificity and high binding affinity against TM with K d determined (0.95 nM). In addition, the aptamer IX has great potential to be employed in the establishment of various aptasensors for TM detection in shellfish products. Furthermore, the CE-SELEX method may provide a universal and convenient method for the aptamer selection against more targets.
研究领域:
食品科学
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分子生物学
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产品关联
DOI
高影响因子
FOOD AND AGRICULTURAL IMMUNOLOGY
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2019
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IF 2.398
Lu Zeng,Shanshan Song,Qiankun Zheng,Pengjie Luo,Xiaoling Wu,Hua Kuang
Shrimp tropomyosin is one of the most important causes of shellfish allergy. The objective of this study was to develop a highly sensitive and specific immunoassay for the detection of shrimp tropomyosin in food. Ten monoclonal antibodies against shrimp tropomyosin were obtained by fusion and cell screening. We found two optimum monoclonal antibodies (mAbs); mAb 2 was used as the capture antibody, and HRP-labelled mAb 3 was used as the detection antibody. Using this pair of mAbs, a sandwich enzyme-linked immunosorbent assay (ELISA) was developed with the limit of detection (LOD) of 0.45 ng/mL. Cross-reactivity with other food allergens using this method was found to be negligible. An immunochromatographic assay strip was also developed for the rapid detection of shrimp tropomyosin with the LOD of 0.5 ng/mL. The results demonstrated that our developmental methods represent a useful tool for the detection of shrimp tropomyosin in food.
研究领域:
免疫学
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食品安全
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生物技术
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产品关联
DOI
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
·
2023
·
IF 4.4
Jun-Hu Cheng,Xinxue Zhang,Ji Ma,Da-Wen Sun
Tropomyosin (TM) is the main allergen in shellfish. Developing a novel, simple and accurate method to track and detect TM in food products is necessary. In this work, a label-free fluorescent aptasensor based on polythymidine (poly(T))-templated copper nanoclusters (CuNCs) was designed for sensitive detection of TM in processed shrimp products. Magnetic beads (MBs), aptamer and cDNA were used to construct an MBs-aptamer@cDNA complex as a detection probe, and with the presence of TM, the poly(T)-templated CuNCs attached at the end of the cDNA as the fluorescent signal was released from the complex to turn on the fluorescence. Under optimal conditions, the poly(T)-templated CuNCs aptasensor achieved a linear range from 0.1 to 50 μg/mL (R 2 = 0.9980), a low limit of detection of 0.0489 μg/mL and an excellent recovery percentage of 105.29%-108.91% in the complex food matrix, providing a new approach for food safety assurance.
研究领域:
食品科学
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纳米技术
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分析化学
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过敏原检测
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Lichun Liu,Ziye Zhang,Zihao Li,Hao Wang,Zhenxing Li,Hong Lin
The incidence of shrimp-induced food allergy is increasing yearly. Glycation has been reported to reduce shrimp tropomyosin (TM) allergenicity, and how advanced glycation end products (AGEs) impact TM allergenicity has garnered worldwide attention. This work investigated the conformational and epitope alterations of TM under α-dicarbonyl compounds (glyoxal (GO), methylglyoxal (MGO), butanedione (BU)) glycation and conformation-allergenicity relationship. As the results, α-dicarbonyl compounds glycation induced high glycation and TM conformational alterations. AGEs glycation sites on TM epitopes were identified by HPLC-MS/MS, with epitope destruction rates of 62.5 %, 50 % and 62.5 % for GO-TM, MGO-TM and BU-TM, respectively. Immunological results revealed TM glycated by α-dicarbonyls compounds performed weaker IgE binding by 33.38–33.86 %, while GO and MGO reduced IgG binding by 63.60 % and 77.72 %, respectively, suggesting α-dicarbonyls compounds reduced TM allergenicity via AGEs-induced epitope loss and conformational changes. This investigation could provide novel insights into how α-dicarbonyls compounds reduce TM allergenicity and prevent shrimp-induced allergy.
研究领域:
免疫学
·
食品科学
·
生物化学
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产品关联
DOI
PubMed
高影响因子
Innovative Food Science & Emerging Technologies
·
2026
·
IF 6.9
Qi Fang,Ashily Liang Wang,Yunzi Jiang,Weiqiang Qiu,Li Li,Yuhui Feng,Yingshan Jin,Chancong Jiang,Yinzhe Jin
This study investigated the mechanism of tropomyosin (TM) immunoreactivity reduction in Litopenaeus vannamei through ohmic heating (OH) combined with glycation. The screening of five common monosaccharides (glucose, xylose, ribose, galactose, and arabinose) and treatment times (0–120 min) revealed that galactose-treated TM samples subjected to OH (50 V/cm, 100 °C) for 60 min exhibited the lowest immunoreactivity. Following the OH–galactose treatment of purified TM and shrimp meat, the IgG/IgE binding capacity of purified TM decreased to 45.65% and 27.16%, respectively. The shrimp meat treatment group exhibited a further reduction in immunoreactivity to 39.99% and 25.75% due to the binding of endogenous sugars in meat with TM during treatment. Structural analysis revealed that there was a decrease in α-helix content, with a transition to β-sheet and random coil conformations, accompanied by reduced intrinsic fluorescence and increased surface hydrophobicity, indicating changes in the secondary and tertiary structures. Notably, the unique rapid volumetric heating characteristics of OH effectively drove these extensive structural modifications. After treatment, the content of amino acids decreased, accompanied by a reduction in the content of allergenic epitope peptides. Furthermore, the gastrointestinal digestibility of the sample was enhanced post-treatment, thereby facilitating human digestion and mitigating potential allergic risks. Molecular docking results demonstrated that galactose primarily binds to TM via glutamate-mediated interactions, which effectively masks the critical antigenic epitopes.
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DOI
高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Lichun Liu,Ziye Zhang,Wei Yang,Fatih Özogul,Zhenxing Li,Hong Lin
α-dicarbonyl compounds are widely present in foods, while their modification effects on food allergens are unclear. This work was conducted to investigate the effects of α-dicarbonyl compounds (glyoxal (GO), methylglyoxal (MGO) and 2, 3-butanedione (BU)) on the digestive stability and intestinal flora of shrimp tropomyosin (TM). As the results, higher α-dicarbonyl concentration, longer time and higher temperature could exacerbate the modification of TM. Compared with TM, GO and MGO significantly reduced the digestive resistance of TM and the IgG-binding capacity of AGEs-TM digests. Although in vitro digestion reduced IgE-binding capacity of TM/AGEs-TM, in vivo evidence (intestinal biopsy and gut microbiota) suggested that they still elicits immune responses. In addition, AGEs-TM could reduce the richness and diversity of intestinal flora, increase the abundance of inflammation-related flora and flora imbalance index, which could provide a new insight into the effects of AGEs on the digestive stability of shrimp tropomyosin and intestinal microbiota.
研究领域:
食品化学
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过敏学
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分子生物学
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营养科学
·
微生物学
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2018
·
IF 4.946
Ziye Zhang,Hang Xiao,Xiaofeng Zhang,Peng Zhou
Tropomyosin (TM) from Exopalaemon modestus was glycoprotein, the effects of deglycosylation (enzyme and chemical regents) and Maillard reaction on the conformation, allergenicity and human cell sensitization of TM were investigated. TM had both N-glycan and O-glycan. After deglycosylation and glycation, the α-helix of TM reduced, while other secondary structures promoted. Deglycosylation enhanced TM allergenicity and digestibility, contributed to digests with lower allergenicity, glucose glycation weakened the allergenicity and digestibility of TM, led to digests with weaker allergenicity. Gastric digestion partly reduced allergenicity of digests, intestinal digestion highly reduced digests’ allergenicity, gastrointestinal digestion most efficiently weakened the allergenicity of digests. After deglycosylation, the deglycosylated TM exerted stronger activation of basophil (KU812), while glucose glycated TM weakened KU812 activation. Deglycosylation exerted inhibition on colon cell (Caco-2) proliferation and increase of IL-8 release, while glucose glycated TM suppressed Caco-2 proliferation and IL-8 release.
研究领域:
食品科学
·
免疫学
·
生物化学
✓ 已验证
DOI
PubMed
高影响因子
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