Phage displayed domain antibody mimics for pyrethroid and its application in immunoassay

Authors

  • Yanyan Zhao 1. School of Food Science and technology, Henan Institute of Science and Technology, Xinxiang 453003, China
  • Ying Liang Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Key Laboratory of Control Technology and Standard for Agri-product Safety and Quality, Ministry of Agriculture and Rural Affairs, Institute of Agricultural Product Quality Safety and Nutrition Research, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China
  • Yuan Liu Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Key Laboratory of Control Technology and Standard for Agri-product Safety and Quality, Ministry of Agriculture and Rural Affairs, Institute of Agricultural Product Quality Safety and Nutrition Research, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China
  • Sicong Tu 4. School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia
  • Shengming Zhao 1. School of Food Science and technology, Henan Institute of Science and Technology, Xinxiang 453003, China
  • Xianjin Liu Key Laboratory of Food Quality and Safety of Jiangsu Province-State Key Laboratory Breeding Base, Key Laboratory of Control Technology and Standard for Agri-product Safety and Quality, Ministry of Agriculture and Rural Affairs, Institute of Agricultural Product Quality Safety and Nutrition Research, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China
  • Kang Tu College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China

Keywords:

domain antibody, enzyme-linked immunosorbent assay, phenoxybenzoic acid, pyrethroid

Abstract

Anti-idiotypic antibodies which can mimic antigens have many potential applications in the immunoassay. This research used the monoclonal antibody of the conserved chemical region of pyrethroids, 3-phenoxybenzoic acid (PBA), and the domain antibody library to develop an environmentally-friendly immunoassay for the detection of pyrethroids. The domain antibodies (A8, B8, and C6) which bound to anti-PBA monoclonal antibody (MAb) were isolated from a naive phage display human domain antibody library. This domain antibody is cloneable, pyrethroid-free, and applicable as a competitive mimetic antigen in the immunoassay. The best immunoassay was achieved using A8, resulting in IC50 of 0.714 μg/mL for PBA, 1.775 μg/mL for Cypermethrin, 1.624 μg/mL for β-cypermethrin, 3.675 μg/mL for Fenvalerate, and 4.895 μg/mL for Flucythrinate. This way of selecting anti-idiotypic antibodies to detect pyrethroids could provide potential applications in developing immunoassays for identifying various chemical contaminants in food. Keywords: domain antibody, enzyme-linked immunosorbent assay, phenoxybenzoic acid, pyrethroid DOI: 10.25165/j.ijabe.20201302.5492 Citation: Zhao Y Y, Liang Y, Liu Y, Tu S C, Zhao S M, Liu X J, et al. Phage displayed domain antibody mimics for pyrethroid and its application in immunoassay. Int J Agric & Biol Eng, 2020; 13(2): 235–240.

References

Ellis D I, Brewster V L, Dunn W B, Allwood J W, Golovanov A P,

Goodacre R. Fingerprinting food: current technologies for the detection of food adulteration and contamination. Chemical Society Reviews, 2012; 41: 5706–5727.

Campàs M, Garibo D, Prieto-Simón B. Novel nanobiotechnological concepts in electrochemical biosensors for the analysis of toxins. Analyst, 2012; 137: 1055–1067.

Cháfer-Pericás C, Maquieira Á, Puchades R. Fast screening methods to detect antibiotic residues in food samples. Trac Trends in Analytical Chemistry, 2010; 29(9): 1038–1049.

Wang Y, Wang Z, Jiang H, Xia X, Shen J, Ding S. Development of a monoclonal antibody-based enzyme-linked immunosorbent assay for the analysis of diclazuril in chicken tissues. Food Analytical Methods, 2013; 6(6): 1685–1692.

Song S, Suryoprabowo S, Liu L, Kuang H, Xu L, Ma W, et al. Development of monoclonal antibody-based colloidal gold immunochromatographic assay for analysis of halofuginone in milk. Food and Agricultural Immunology, 2019; 30(1): 112–122.

Xu Y, Chen B, He Q H, Qiu Y L, Liu X, He Z Y, et al. New approach for development of sensitive and environmentally friendly immunoassay for Mycotoxin Fumonisin B1 based on using Peptide-MBP fusion protein as substitute for coating antigen. Analytical Chemistry, 2014; 86: 8433–8440.

Xu Y, He Z, He Q, Qiu Y, Chen B, Chen J, et al. Use of cloneable peptide–mbp fusion protein as a mimetic coating antigen in the standardized immunoassay for Mycotoxin Ochratoxin A. Journal of Agricultural and Food Chemistry, 2014; 62: 8830–8836.

Shestowsky W S, Holmes C, Hu T, Marr J, Wright J, Chin J, et al. An anti-okadaic acid-anti-idiotypic antibody bearing an internal image of okadaic acid inhibits protein phosphatase PP1 and PP2A catalytic activity. Biochemical and Biophysical Research Communications, 1993; 192: 302–310.

Chanh T C, Rappocciolo G, Hewetson J F. Monoclonal anti-idiotype induces protection against the cytotoxicity of the trichothecene mycotoxin T-2. Journal of Immunology, 1990; 144: 4721–4728.

Yu F Y, Chu F S. Production and characterization of a monoclonal anti-anti-idiotype antibody against fumonisin B1. Journal of Agricultural and Food Chemistry, 1999; 47: 4815–4820.

Guan D, Li P, Cui Y, Zhang Q, Zhang W. A competitive immunoassay with a surrogate calibrator curve for aflatoxin M 1 in milk. Analytica Chimica Acta, 2011; 703: 64–69.

Smith G P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science, 1985; 228: 1315–1317.

Wang Y, Wang H, Li P, Zhang Q, Kim H J, Gee S J, et al. Phage-displayed peptide that mimics aflatoxins and its application in immunoassay. Journal of Agricultural and Food Chemistry, 2013; 61: 2426–2433.

Wang Y, Li P, Majkova Z, Bever C R, Kim H J, Zhang Q, et al. Isolation of alpaca anti-idiotypic heavy-chain single-domain antibody for the aflatoxin immunoassay. Analytical Chemistry, 2013; 85: 8298–8303.

Liu R, Yu Z, He Q, Xu Y. An immunoassay for ochratoxin A without the mycotoxin. Food Control, 2007; 18: 872–877.

Nejad S M, Veldhuis S L, Richard G, Hall J C. Selection of single chain variable fragment (scFv) antibodies from a hyperimmunized phage display library for the detection of the antibiotic monensin. Journal of Immunological Methods, 2010; 360: 103–118.

González-Techera A, Zon M A, Molina P G, Fernández H, González-Sapienza G, Arévalo F J. Development of a highly sensitive noncompetitive electrochemical immunosensor for the detection of atrazine by phage anti-immunocomplex assay. Biosensors and Bioelectronics, 2015; 64: 650–656.

Yin W, Hua X, Liu X, Shi H, Gee S J, Wang M, Hammock B D. Development of an enzyme-linked immunosorbent assay for thiacloprid in soil and agro-products with phage-displayed peptide. Analytical Biochemistry, 2015; 481: 27–32.

Yuan Q, Pestka J J, Hespenheide B M, Kuhn L A, Linz J E, Hart L P. Identification of mimotope peptides which bind to the mycotoxin deoxynivalenol-specific monoclonal antibody. Appl. Environmental Microbiology, 1999; 65: 3279–3286.

He Q H, Xu Y, Huang Y H, Liu R R, Huang Z B, Li Y P. Phage-displayed peptides that mimic zearalenone and its application in immunoassay. Food Chemistry, 2011; 126: 1312–1315.

Li Y, Sun Y, Beier R, Lei H, Gee S, Hammock B, et al. Immunochemical techniques for multianalyte analysis of chemical residues in food and the environment: A review. Trac-Trends in Analytical Chemistry, 2017; 88: 25–40.

Li C, Luo X, Li Y, Yang H, Liang X, Wen K, et al. A class-selective immunoassay for sulfonamides residue detection in milk using a superior polyclonal antibody with broad specificity and highly uniform affinity. Molecules, 2019; 24(3): 443.

Wen M T, Liu Y, Yan S, Zhang X, Wang H, Liu X J. Production and identification of broad spectrum monoclonal antibody against a group of pyrethroid insecticides. Chinese Journal of Analytical Chemistry, 2014, 42(9): 1245–1251. (in Chinese)

Lee C M Y, Niccolo I, Frederic S, Daniel C. Selection of human antibody fragments by phage display. Nature Protocols, 2007; 2: 3001–3008.

Zhang Q, Zhang W, Wang X. Immunoassay development for the class-specific assay for types I and II pyrethroid insecticides in water samples. Molecules, 2010; 15: 164–177.

Delaunay-Bertoncini N, Pichon V, Hennion M C. Experimental comparison of three monoclonal antibodies for the class-selective immunoextraction of triazines: Correlation with molecular modeling and principal component analysis studies. Journal of Chromatography A, 2003; 999: 3–15.

Ahn K C, Kim H-J, McCoy M R, Gee S J, Hammock B D. Immunoassays and biosensors for monitoring environmental and human exposure to pyrethroid insecticides. Journal of Agricultural and Food Chemistry, 2010; 59: 2792–2802.

Vanderlaan M, Stanker L, Watkins B. Immunoassays for trace chemical analysis: monitoring toxic chemicals in humans, food, and the environment; American Chemical Society; Washington, DC, 1991; Paper No. 2–13.

Downloads

Published

2020-04-10

How to Cite

Zhao, Y., Liang, Y., Liu, Y., Tu, S., Zhao, S., Liu, X., & Tu, K. (2020). Phage displayed domain antibody mimics for pyrethroid and its application in immunoassay. International Journal of Agricultural and Biological Engineering, 13(2), 235–240. Retrieved from https://ijabe.migration.pkpps06.publicknowledgeproject.org/index.php/ijabe/article/view/5492

Issue

Vol. 13 No. 2 (2020): IJABE

Section

Agro-product and Food Processing Systems

License

IJABE is an international peer reviewed, open access journal, adopting Creative Commons Copyright Notices as follows.

Authors who publish with this journal agree to the following terms:

  1. Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
  2. Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
  3. Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).