Special Issue "Monoclonal Antibody Preparation against Natural Product and Its Application"

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A special issue of Antibodies (ISSN 2073-4468).

Deadline for manuscript submissions: closed (31 August 2012)

Special Issue Editor

Guest Editor
Prof. Dr. Yukihiro Shoyama

Professor, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, Japan
Website | E-Mail
Phone: +81-956-20-5653
Fax: (+81) 956-20-5622
Interests: monoclonal antibodies; bioactive compounds; marihuana study; isolation and structure elucidation; biotechnology

Special Issue Information

Dear Colleagues,

As the rapid development of the molecular biosciences and their biotechnological application, immunoassay system using monoclonal antibody (MAb) against drugs and bioactive natural products having small molecular weight have become important tools for studies on quantitative and/or qualitative analytical techniques, enzyme assay and receptor binding analysis owing to their specific affinity. However, since direct immunization for small molecular natural product is impossible, conjugate synthesis of natural products with carrier protein is necessary at the first step. MAb can be successful obtained by immunization of mice, hybridoma preparation, selection and cloning of hybridoma and culturing. Although high specific MAb in general will be required, wide-cross reactive MAb is also useful for analysis of total related components. Qualitative and quantitative analysis of bioactive natural product is necessary for the quality control of herbal medicines. Immunostaining like eastern blotting can determine and identify bioactive compounds specifically in crude extract resulting in fingerprinting of herb medicine. Compact MAb, Fc-engineered antibody can be used as a neutralized antibody for the plant breeding. A special issues with focus on “Monoclonal Antibody Preparation against Natural Product and Its Application” will review recent developments and application of MAbs against natural products having small molecule and further accelerate the investigation around MAb against natural product.

Prof. Dr. Yukihiro Shoyama
Guest Editor

Keywords

  • monoclonal antibody
  • natural product having small molecule
  • ELISA
  • quantitative and qualitative analysis
  • finger print analysis
  • eastern blotting
  • immunoaffinity column
  • single chain Fv
  • Fc-engineered antibody

Published Papers (8 papers)

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Research

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Open AccessCommunication Generation of a Monoclonal Antibody Specifically Reacting with Neuron-specific TATA-Box Binding Protein-Associated Factor 1 (N-TAF1)
Antibodies 2013, 2(1), 1-8; doi:10.3390/antib2010001
Received: 9 November 2012 / Revised: 10 December 2012 / Accepted: 14 December 2012 / Published: 21 December 2012
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Abstract
TATA-box binding protein-associated factor 1 (TAF1), the largest subunit of the transcription factor IID complex, plays an important role in the RNA polymerase II-mediated gene transcription pathway regulating the transcription of a large number of genes related to cell division. The neuron-specific isoform
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TATA-box binding protein-associated factor 1 (TAF1), the largest subunit of the transcription factor IID complex, plays an important role in the RNA polymerase II-mediated gene transcription pathway regulating the transcription of a large number of genes related to cell division. The neuron-specific isoform of the TAF1 gene (N-TAF1) may have an essential role in neurons through transcriptional regulation of many neuron-specific genes. The present study reports the preparation and properties of a monoclonal antibody directed against N-TAF1. The monoclonal antibody, 3A-11F, specifically recognized N-TAF1 protein with no reactivity to TAF1 protein, as evidenced by immunocytochemistry and immunoprecipitation using cultured cells expressing recombinant N-TAF1 or TAF1 protein. Immunohistochemistry using 3A-11F showed that N-TAF1-imunoreactivity was detected in the nuclear region of neurons in the rat brain. The 3A-11F monoclonal antibody promises to be a useful tool for determining the expression pattern and biological function of N-TAF1 in the brain. Full article
Open AccessArticle Development of Eastern Blotting Technique for Analysis of Baicalin Using Anti-Baicalin Monoclonal Antibody
Antibodies 2012, 1(3), 284-293; doi:10.3390/antib1030284
Received: 31 August 2012 / Revised: 18 November 2012 / Accepted: 22 November 2012 / Published: 27 November 2012
Cited by 2 | PDF Full-text (634 KB) | HTML Full-text | XML Full-text
Abstract
Scutellariae radix (S. radix) is one of the most important crude drugs used in Kampo medicines (KMs). A part of its pharmaceutical properties is due to flavone glycoside, baicalin (BI). A technique named eastern blotting was developed for the specific and
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Scutellariae radix (S. radix) is one of the most important crude drugs used in Kampo medicines (KMs). A part of its pharmaceutical properties is due to flavone glycoside, baicalin (BI). A technique named eastern blotting was developed for the specific and easy identification of BI in the extracts of crude drugs and KMs using anti-BI monoclonal antibody (MAb). BI separated by silica gel thin-layer chromatography (TLC) transferred to a polyethersulfone (PES) membrane was treated with a NaIO4 solution and reacted with bovine serum albumin (BSA) preparing BI-BSA conjugate on the PES membrane. Anti-BI MAb was bound and then antibody labeled with peroxidase directed against anti-BI MAb. Finally, a substrate was added and then BI was detected. As little as 1 mg of BI was still detected on the PES membrane under immunostaining method. Various samples of S. radix and KMs which contain S. radix were qualitatively analyzed, and BI was visually detected by eastern blotting technique. Furthermore, this method was applied for the immunohistochemical study to investigate the distribution of BI in the fresh root of Scutellaria baicalensis using immunoblotting by transferred from fresh root to the PES membrane. Full article
Open AccessArticle Quality Control System for Beer Developed with Monoclonal Antibodies Specific to Barley Lipid Transfer Protein
Antibodies 2012, 1(3), 259-272; doi:10.3390/antib1030259
Received: 17 September 2012 / Revised: 28 September 2012 / Accepted: 9 October 2012 / Published: 16 October 2012
Cited by 1 | PDF Full-text (607 KB) | HTML Full-text | XML Full-text
Abstract
Non-specific lipid transfer protein (LTP) in barley grain reacted with the IgE in sera drawn from food allergy patients. A sandwich-type of enzyme-linked immunosorbent assay (ELISA) was developed with mouse monoclonal antibodies raised against LTP purified with barley flour. This ELISA showed a
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Non-specific lipid transfer protein (LTP) in barley grain reacted with the IgE in sera drawn from food allergy patients. A sandwich-type of enzyme-linked immunosorbent assay (ELISA) was developed with mouse monoclonal antibodies raised against LTP purified with barley flour. This ELISA showed a practical working range of 0.3–3 ng/mL and no cross-reactivity with wheat, adlay and rye. Using this ELISA, LTP was determined in several types of barley-foods, including fermented foods such as malt vinegar, barley-malt miso and beer. LTP content in beer of the same kind was approximately constant, even if manufacturing factory and production days were different. Not only as a factor of foam formation and stability but also as an allergen, controlling and monitoring of LTP in beer should be considered. Taken together, our LTP-detecting ELISA can be proposed as an appropriate system for the quality control of beer. Full article

Review

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Open AccessReview Developments and Challenges for mAb-Based Therapeutics
Antibodies 2013, 2(3), 452-500; doi:10.3390/antib2030452
Received: 23 May 2013 / Revised: 18 July 2013 / Accepted: 2 August 2013 / Published: 16 August 2013
Cited by 20 | PDF Full-text (867 KB) | HTML Full-text | XML Full-text
Abstract
The continuous increase in the number of approved monoclonal antibody (mAb)-based therapy suggests that mAbs, and their derivatives, will continue to be the focus of the biotherapeutics industry for years to come. Although vast improvements in our capability to manufacture, characterize, and stabilize
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The continuous increase in the number of approved monoclonal antibody (mAb)-based therapy suggests that mAbs, and their derivatives, will continue to be the focus of the biotherapeutics industry for years to come. Although vast improvements in our capability to manufacture, characterize, and stabilize mAbs have been achieved, there are still challenges to be overcome. These include analytical and stabilization approaches associated with the development of high concentration mAb formulations. In addition, several mAb-based modalities are under development, including antibody drug conjugates (ADCs), fusion proteins, and bispecific antibodies (bsAbs), all designed to overcome the limitations encountered with mAb therapy. The current status of their development, with emphasis on manufacturing challenges as well as preliminary clinical results, will be reviewed. Full article
Open AccessReview Preparation of Knockout Extract by Immunoaffinity Column and Its Application
Antibodies 2012, 1(3), 294-307; doi:10.3390/antib1030294
Received: 28 August 2012 / Revised: 30 November 2012 / Accepted: 4 December 2012 / Published: 6 December 2012
Cited by 1 | PDF Full-text (355 KB) | HTML Full-text | XML Full-text
Abstract
Importance of herbal medicines have recently increased owing to rising interest in their health benefits. However, medicinal plant extracts are complex mixtures of phytochemicals that act synergistically or additively on specific and/or multiple molecular and cellular targets. Thus, it is difficult to examine
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Importance of herbal medicines have recently increased owing to rising interest in their health benefits. However, medicinal plant extracts are complex mixtures of phytochemicals that act synergistically or additively on specific and/or multiple molecular and cellular targets. Thus, it is difficult to examine the actual pharmacological roles of active compounds in plant extracts. This review describes a new strategy for isolating target compounds from plant extracts using immunoaffinity columns coupled with monoclonal antibodies (mAbs) against natural compounds. Through one-step purification using mAb-coupled immunoaffinity columns, we succeeded in preparing a knockout (KO) extract, which contains all components except the target compound. Furthermore, we investigated the pharmacological effects of the KO extract to reveal the actual effects of a bioactive compound in the crude extract. This approach may help determine the potential function of target compounds in herbal medicines. Full article
Open AccessReview Immunochemical Analysis of the Antimalarial Drugs Artemisinin and Artesunate
Antibodies 2012, 1(3), 273-283; doi:10.3390/antib1030273
Received: 3 September 2012 / Revised: 19 October 2012 / Accepted: 29 October 2012 / Published: 2 November 2012
Cited by 1 | PDF Full-text (249 KB) | HTML Full-text | XML Full-text
Abstract
We prepared a monoclonal antibody (mAb 1C1) showing specificity for artemisinin (AM) and artesunate (AS), and we developed an indirect competitive enzyme-linked immunosorbent assay (icELISA) using this novel mAb. Moreover, we prepared a recombinant antibody derived from mAb 1C1 in order to overcome
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We prepared a monoclonal antibody (mAb 1C1) showing specificity for artemisinin (AM) and artesunate (AS), and we developed an indirect competitive enzyme-linked immunosorbent assay (icELISA) using this novel mAb. Moreover, we prepared a recombinant antibody derived from mAb 1C1 in order to overcome insufficient mAb production by hybridoma culture. A recombinant antigen-binding fragment (Fab) was easily constructed using antibody manipulation technologies and was produced by microorganisms in high yield. We herein review immunochemical approaches for analysis of the antimalarial drugs AM and AS that were able to yield analysis results for multiple samples in a short period of time using simple and reliable protocols. Full article
Open AccessReview Fluobodies against Bioactive Natural Products and their Application in Fluorescence-Linked Immunosorbent Assay
Antibodies 2012, 1(2), 239-258; doi:10.3390/antib1020239
Received: 7 August 2012 / Revised: 27 August 2012 / Accepted: 28 August 2012 / Published: 11 September 2012
Cited by 7 | PDF Full-text (1074 KB) | HTML Full-text | XML Full-text
Abstract
An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (MAb), Fab antibody, and single-chain variable fragment (scFv) antibody has become one of the most promising analytical methods owing to its rapidity, sensitivity, and reliability. Recently, a chimera of green fluorescent protein (GFP) with a
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An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (MAb), Fab antibody, and single-chain variable fragment (scFv) antibody has become one of the most promising analytical methods owing to its rapidity, sensitivity, and reliability. Recently, a chimera of green fluorescent protein (GFP) with a scFv antibody, named fluobody, was proposed as a probe for an alternative immunosorbent assay; i.e., fluorescence-linked immunosorbent assay (FLISA). In this FLISA, an even more sensitive, simple, and rapid immunoassay can be performed by detecting the highly sensitive fluorophore of GFP that is genetically and directly fused to the scFv antibody. In addition, the time- and cost-consuming secondary antibody reaction and the following enzyme-substrate reaction, necessary for conventional ELISA, can be avoided, making it possible to complete the assay more rapidly. Focusing on naturally occurring bioactive products, fluobody recognizing 1,4-naphthoquinone, plumbagin and triterpenoid saponin, ginsenosides were successfully expressed in Escherichia coli (E. coli) and applied to FLISA. The construction, the expression, and the potential use of fluobody in quantitative/qualitative analysis of bioactive natural products are reviewed in this article. Full article
Open AccessReview Refolding Technology for scFv Using a New Detergent, N-Lauroyl-L-glutamate and Arginine
Antibodies 2012, 1(2), 215-238; doi:10.3390/antib1020215
Received: 10 July 2012 / Revised: 16 August 2012 / Accepted: 21 August 2012 / Published: 29 August 2012
Cited by 1 | PDF Full-text (428 KB) | HTML Full-text | XML Full-text
Abstract
Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding
[...] Read more.
Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding sites, is extensively investigated. It becomes increasingly apparent, however, that these smaller fragments of antibodies are rather difficult to produce, as the normally efficient mammalian secretion system does not work well for these fragments. Thus, refolding of insoluble proteins produced in Escherichia coli is a method of choice, although such refolding is mainly based on trial-and-error experiment. Here we describe a novel refolding system using a new amino acid-based detergent, N-lauroyl-L-glutamate, and arginine. This detergent appears to readily dissociate from proteins below critical micelle concentration (CMC), while remaining effective in protein solubilization above CMC. Arginine suppresses protein aggregation when the detergent concentration was reduced below CMC. The interaction of the detergent and arginine with proteins, which play an important role in protein refolding, will be discussed in great length. Full article

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