Development of an enzyme-linked immunosorbent assay for the detection of nitrofurantoin metabolite, 1-amino-hydantoin, in animal tissues

Jiang, Wenxiao; Luo, Pengjie; Wang, Xia; Chen, Xia; Zhao, Yunfeng; Wei, Shi; Wu, Xiaoping; Wu, Yongning; Shen, Jianzhong

doi:10.1016/j.foodcont.2011.05.014

Cited by 64 publications

(48 citation statements)

References 22 publications

(38 reference statements)

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“…For nitrofuran metabolites, haptens were always designed by derivatising the metabolites with 3-CBA or 4-CBA [6,7,[9][10][11][12][13][14][15]. Although this strategy was able to generate antibodies with high specificity and sensitivity, it's believed that there are some other strategies to further improve the antibody characteristics.…”

Section: Design and Synthesis Of Haptensmentioning

confidence: 99%

“…The first enzyme-linked immunosorbent assay (ELISA) capable of detecting the furazolidone metabolite (AOZ) was developed by Cooper et al [6] under the support of a multi-national EU research project "FoodBRAND" [2]. Since then, immunoassays for the determination of AOZ [7][8][9], SEM [10][11][12], AHD [13,14] and AMOZ [15] were reported in succession.…”

Section: Introductionmentioning

confidence: 99%

“…NPAOZ, NASEM, NPAHD and NPAMOZ) [6][7][8][9][10][11][12][13][14][15]. In most studies, nitrofuran metabolites were derivatised with 3-carboxybenzaldehyle (3-CBA) or 4-carboxybenzaldehyle (4-CBA) to form immunizing haptens [6,7,[9][10][11][12][13][14][15].…”

Section: Introductionmentioning

confidence: 99%

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Novel hapten synthesis for antibody production and development of an enzyme-linked immunosorbent assay for determination of furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ)

Shen

Sun

et al. 2013

Talanta

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Publisher rights This is the author's version of a work that was accepted for publication in Talanta. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Talanta, VOL 103, 01/2012 General rights Copyright for the publications made accessible via the Queen's University Belfast Research Portal is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Cite this article as: Zhen-Lin Xu, Yu-Dong Shen, Yuan-Ming Sun, Katrina Campbell, Yuan-Xin Tian, Shi-Wei Zhang, Hong-Tao Lei and Yue-Ming Jiang, Novel hapten synthesis for antibody production and development of an enzyme-linked immunosorbent assay for determination of furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ), Talanta, http://dx.doi.org/10. 1016/j.talanta.2012.10.059 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting galley proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. AbstractA heterologous competitive indirect enzyme-linked immunosorbent assay (ciELISA) for the determination of the furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ) was developed. AMOZ was derivatised with 2-(4-formylphenoxy)acetic acid or 2-(3-formylphenoxy)acetic acid to obtain two novel immunizing haptens. The ability of these haptens in producing specific polyclonal antibodies against the nitrophenyl derivative of AMOZ (NPAMOZ) was compared with that of traditional immunizing haptens (derivatised AMOZ with 3-carboxybenzaldehyle or 4-carboxybenzaldehyle). The results indicated that the novel immunizing haptens were able to produce antibodies with almost a two-fold improvement in sensitivity of the ciELISA for NPAMOZ in comparison with the existing antibody based ELISAs. The differences in sensitivity were explained by the molecular modeling of the lowest energy conformations of NPAMOZ and the haptens. Another novel hapten, derivatised AMOZ with 2-oxoacetic acid, was synthesized and used as a heterologous coating hapten. The results showed that this strategy of using only a partial structure of the target molecule as the coating hapten was able to obtain a two to three-fold improvement in sensitivity. This study provided a modern approach for the development of an immunoassay with improved sensitivity for the metabolites of nitrofuran antibiotics.

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Section: Design and Synthesis Of Haptensmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Novel hapten synthesis for antibody production and development of an enzyme-linked immunosorbent assay for determination of furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ)

Shen

Sun

et al. 2013

Talanta

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“…The coating antigen, antibody concentrations, and incubation temperature were optimized according to a previous research (Jiang et al 2012). The optimum working concentrations of AFB 1 -OVA and MAb were optimized using checkerboard titration gradient dilution.…”

Section: Development Of An Indirect Competitive Elisamentioning

confidence: 99%

“…Six serial diluted standard curves were performed in the icELISA, and the competition curves were graphed and fitted by a four-parameter logistic equation. The 50 % inhibition concentration (IC 50 ) values of different aflatoxins were determined, and the cross-reactivity was obtained by comparing the IC 50 values of analytes with the following formula: cross-reactivity (%)0[IC 50 (AFB 1 )/IC 50 (analyte)]×100 (Jiang et al 2012).…”

Section: Development Of An Indirect Competitive Elisamentioning

confidence: 99%

Simultaneous Determination of Aflatoxin B1 and Aflatoxin M1 in Food Matrices by Enzyme-Linked Immunosorbent Assay

et al. 2012

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Aflatoxins are a class of highly toxic chemical contaminants occurring in food. Consumption of aflatoxincontaminated food can lead to harmful effects on human health. A rapid and reliable analysis of aflatoxins in food is crucial. In this study, we generated a broad-specific monoclonal antibody (MAb) 3 C10 against aflatoxin B 1 (AFB 1 ). The MAb 3 C10 binds specifically to AFB 1 and AFM 1 and has a IC 50 of 0.13 μg L −1 for AFB 1 and 0.16 μg L −1 for AFM 1 . Furthermore, the MAb showed high cross-reactivity to AFB 2 , AFG 1 , and AFG 2 . To enable simultaneous AFB 1 and AFM 1 detection in different food matrices, an indirect competitive enzyme-linked immunosorbent assay (icELISA) based on MAb 3 C10 has been developed and optimized. In addition, the extraction methods of different food matrices (peanut, corn, soybean, wheat flour, rice, soy sauce, vinegar, wine, raw milk, pure milk, skimmed milk, and yogurt) were established. The average recovery ranged from 73 to 121 %, with relative standard deviation values less than 15 %. The limit of detection was 0.52+0.36 μg kg −1 (mean+3SD) for AFB 1 in eight agricultural products and 0.031+0.015 μg kg −1 (mean+3SD) for AFM 1 in four dairy products. The sensitivity of icELISA was below the limit set by the European Commission for aflatoxin detection in different food matrices and similar to LC-MS/MS method. We demonstrate a rapid, simple, and reliable method for simultaneous screening of AFB 1 and AFM 1 in different food matrices.

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Enhanced targeting: Production of filamentous bacteriophage monoclonal antibodies using the major coat protein pVIII as anchor

Li,

Zhu,

Yuan

et al. 2024

Biotechnology Journal

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Filamentous bacteriophage display technology has been employed in antibody discovery, drug screening, and protein–protein interaction study across various fields, including food safety, agricultural pollution, and environmental monitoring. Antifilamentous bacteriophage antibodies for identifying filamentous bacteriophage are playing a pivotal role in this technology. However, the existing antifilamentous bacteriophage antibodies lack sensitivity and specificity, and the antibodies preparation methods are cumbersome and hyposensitive. The major coat protein pVIII of filamentous bacteriophage has an advantage in quantification, which is benefit for detecting signal amplification but its full potential remains underutilized. In this study, the partial polypeptide CT21 of the major coat protein pVIII of filamentous bacteriophage was intercepted as the targeted immunogen or coating antigen to prepare antifilamentous bacteriophage antibodies. Six filamentous bacteriophage‐specific monoclonal antibodies (mAbs) M5G8, M9A2, P6B5, P6D2, P8E4, and P10D4 were obtained. The limit of detections of the prepared six mAbs for detecting filamentous bacteriophage was 1.0 × 107 pfu mL−1. These mAbs stayed stable under different pH, temperature, and exhibited high specificity in real application. This study not only provides a new idea for simplifying the preparation of antifilamentous bacteriophage antibodies which could apply in filamentous bacteriophage display, but it also presents a novel strategy for preparing antibodies against protein‐specific epitopes with high sensitivity.

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Development of an enzyme-linked immunosorbent assay for the detection of nitrofurantoin metabolite, 1-amino-hydantoin, in animal tissues

Cited by 64 publications

References 22 publications

Novel hapten synthesis for antibody production and development of an enzyme-linked immunosorbent assay for determination of furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ)

Novel hapten synthesis for antibody production and development of an enzyme-linked immunosorbent assay for determination of furaltadone metabolite 3-amino-5-morpholinomethyl-2-oxazolidinone (AMOZ)

Simultaneous Determination of Aflatoxin B1 and Aflatoxin M1 in Food Matrices by Enzyme-Linked Immunosorbent Assay

Enhanced targeting: Production of filamentous bacteriophage monoclonal antibodies using the major coat protein pVIII as anchor

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