Generation of a monoclonal antibody that has reduced binding activity to VX-inactivated butyrylcholinesterase (BuChE) compared to BuChE by phage display

Yoon, Jun-Yeol; Kim, Dong Hwan; Kim, Sangkyu; Kim, Dain; Jo, Gyunghee; Shin, Moon-Sik; Yoo, Jeongha; Kang, Heui Keun; Kim, Min Soo; Kim, Young‐Jin; Lee, Nam-Taek; Hong, Hyo Jeong; Kim, Yoon-Won

doi:10.1007/s12257-017-0110-7

Cited by 8 publications

(6 citation statements)

References 25 publications

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“…It is conceivable that this is a promising and cost-effective method because of quick response, reliability and low maintenance cost [5, 26, 27, 31, 32, 33]. As described in the literatures, the antibodies required for current immunoassays relatively expensive, especially for multiplexed assays or the testing of multiple samples [1, 5, 16, 27, 34, 35]. Therefore, unique peptides are becoming increasingly popular as effective affinity reagents, in place of antibodies, in the development of new biosensors.…”

Section: Introductionmentioning

confidence: 99%

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Development of peptide biosensor for the detection of dengue fever biomarker, nonstructural 1

et al. 2019

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Dengue virus (DENV) nonstructural 1 (NS1) protein is a specific and sensitive biomarker for the diagnosis of dengue. In this study, an efficient electrochemical biosensor that uses chemically modified affinity peptides was developed for the detection of dengue virus NS1. A series of amino acid-substituted synthetic peptides was rationally designed, chemically synthesized and covalently immobilized to a gold sensor surface. The sensor performance was monitored via square wave voltammetry (SWV) and electrochemical impedance spectroscopy (EIS). Potential affinity peptides specific for NS1 were chosen according to the dynamic current decrease in SWV experiments. Using circular dichroism, the molar ellipticity of peptides (DGV BP1–BP5) was determined, indicating that they had a mostly similar in random coil structure, not totally identical. Using SWV, DGV BP1 was selected as a promising recognition peptide and limit of detection for NS1 was found to be 1.49 μg/mL by the 3-sigma rule. DGV BP1 showed good specificity and stability for NS1, with low signal interference. The validation of the sensor to detect NS1 proteins was confirmed with four dengue virus culture broth (from serotype 1 to 4) as proof-of-concept. The detection performance of our sensor incorporating DGV BP1 peptides showed a statistically significant difference. These results indicate that this strategy can potentially be used to detect the dengue virus antigen, NS1, and to diagnosis dengue fever within a miniaturized portable device in point-of-care testing.

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Section: Introductionmentioning

confidence: 99%

“…Evolutionary phage display is a well-characterized method for screening unique affinity peptides that specifically bind targets of interest [32, 35]. Using this approach, our group recently reported a new electrochemical phage-based sensor for the detection of various targets [37–40].…”

Section: Introductionmentioning

confidence: 99%

Development of peptide biosensor for the detection of dengue fever biomarker, nonstructural 1

et al. 2019

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“…ScFv fragments often have a high tendency to form multimers as well as aggregates and have been found to lose affinity during conversion to Ig (immunoglobulin)G, whereas Fab fragments have been found to possess comparably higher structural stability by the presence of the CH1 and light-chain constant domain (CL), and thus their binding activities were retained after conversion to IgG [32]. We previously generated a human synthetic Fab library based on the VH3-23 and VK1-39 framework pairing and have successfully generated mAbs against recombinant proteins and peptide [33][34][35] In this study, to generate mAbs against the serotype-specific LPS of V. cholerae, we exploited the advantages of phage display technology. We efficiently generated anti-Ogawa mAbs from a human synthetic Fab library and confirmed that they bind to V. cholerae vaccine in a dose-dependent fashion.…”

Section: Vibrio Cholerae Cause Of the Life-threatening Diarrheal Dismentioning

confidence: 99%

Generation and Characterization of Monoclonal Antibodies to the Ogawa Lipopolysaccharide of Vibrio cholerae O1 from Phage-Displayed Human Synthetic Fab Library

Kim

Hong

Choi

et al. 2020

J. Microbiol. Biotechnol.

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Vibrio cholerae , cause of the life-threatening diarrheal disease cholera, can be divided into different serogroups based on the structure of its lipopolysaccharide (LPS), which consists of lipid-A, corepolysaccharide and O-antigen polysaccharide (O-PS). The O1 serogroup, the predominant cause of cholera, includes two major serotypes, Inaba and Ogawa. These serotypes are differentiated by the presence of a single 2- O -methyl group in the upstream terminal perosamine of the Ogawa O-PS, which is absent in the Inaba O-PS. To ensure the consistent quality and efficacy of the current cholera vaccines, accurate measurement and characterization of each of these two serotypes is highly important. In this study, we efficiently screened a phage-displayed human synthetic Fab library by bio-panning against Ogawa LPS and finally selected three unique mAbs (D9, E11, and F7) that specifically react with Ogawa LPS. The mAbs bound to Vibrio cholerae vaccine in a dose-dependent fashion. Sequence and structure analyses of antibody paratopes suggest that IgG D9 might have the same fine specificity as that of the murine mAbs, which were shown to bind to the upstream terminal perosamine of Ogawa O-PS, whereas IgGs F7 and E11 showed some different characteristics in the paratopes. To our knowledge, this study is the first to demonstrate the generation of Ogawa-specific mAbs using phage display technology. The mAbs will be useful for identification and quantification of Ogawa LPS in multivalent V. cholerae vaccines.

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“…For indirect ELISA, 100 ng of BSA, Bio-preS1-L peptide, preS1(1-119), or recombinant preS1 was used as an immobilized antigen and horseradish peroxidase (HRP)conjugated anti-M13 (1:5,000 (v/v); GE Healthcare, USA) as a secondary antibody. For quantitative ELISA, anti-M13 antibody (100 ng/well, GE Healthcare, USA) and anti-human kappa-HRP (1:2,000 (v/v); Novex, USA) were used as the immobilized antigen and secondary antibody, respectively, as described previously [17].…”

Section: Selection Of Pres1-specific Fab From a Phage-displayed Humanmentioning

confidence: 99%

Generation and Characterization of a Neutralizing Human Monoclonal Antibody to Hepatitis B Virus PreS1 from a Phage-Displayed Human Synthetic Fab Library

Jo¹,

Jeong²,

Wi³

et al. 2018

Journal of Microbiology and Biotechnology

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Generation of a monoclonal antibody that has reduced binding activity to VX-inactivated butyrylcholinesterase (BuChE) compared to BuChE by phage display

Cited by 8 publications

References 25 publications

Development of peptide biosensor for the detection of dengue fever biomarker, nonstructural 1

Development of peptide biosensor for the detection of dengue fever biomarker, nonstructural 1

Generation and Characterization of Monoclonal Antibodies to the Ogawa Lipopolysaccharide of Vibrio cholerae O1 from Phage-Displayed Human Synthetic Fab Library

Generation and Characterization of a Neutralizing Human Monoclonal Antibody to Hepatitis B Virus PreS1 from a Phage-Displayed Human Synthetic Fab Library

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