ArticleJournal of immunological methods2011
Comparison of the efficiency of antibody selection from semi-synthetic scFv and non-immune Fab phage display libraries against protein targets for rapid development of diagnostic immunoassays.
Article in Journal of immunological methods, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Integrating fab phage and yeast display through seamless transfer of paired heavy- and light-chain libraries for efficient antibody discovery.Antibody therapeutics · 2026Article
- Phage Display Technology: Design, Library Construction, and Panning Strategies for Antibody Development.Biomolecules & therapeutics · 2026Review
- Generation and Next-Generation Sequencing-Based Characterization of a Large Human Combinatorial Antibody Library.International journal of molecular sciences · 2023Article
- A Patent Review on the Therapeutic Application of Monoclonal Antibodies in COVID-19.International journal of molecular sciences · 2021Review
- Article
- Directing evolution of novel ligands by mRNA display.Chemical Society reviews · 2021Review
- Antibody Identification for Antigen Detection in Formalin-Fixed Paraffin-Embedded Tissue Using Phage Display and Naïve Libraries.Antibodies (Basel, Switzerland) · 2021Review
- Golden Gate assembly with a bi-directional promoter (GBid): A simple, scalable method for phage display Fab library creation.Scientific reports · 2020Article
- Development of therapeutic antibodies for the treatment of diseases.Journal of biomedical science · 2020Review
- Phage Display Derived Monoclonal Antibodies: From Bench to Bedside.Frontiers in immunology · 2020Review
- Fab is the most efficient format to express functional antibodies by yeast surface display.mAbs · 2018Article
- Article
- A novel anti-p21Ras scFv antibody reacting specifically with human tumour cell lines and primary tumour tissues.BMC cancer · 2016Article
- Selection of scFv Antibody Fragments Binding to Human Blood versus Lymphatic Endothelial Surface Antigens by Direct Cell Phage Display.PloS one · 2015Article
- Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications.Journal of translational medicine · 2014Article
- The role of phage display in therapeutic antibody discovery.International immunology · 2014Review
- The selection performance of an antibody library displayed on filamentous phage coat proteins p9, p3 and truncated p3.BMC research notes · 2014Article
- In vitro Fab display: a cell-free system for IgG discovery.Protein engineering, design & selection : PEDS · 2014Article
- Novel phage display-derived mycolic acid-specific antibodies with potential for tuberculosis diagnosis.Journal of lipid research · 2013Article
- Phage display--a powerful technique for immunotherapy: 1. Introduction and potential of therapeutic applications.Human vaccines & immunotherapeutics · 2012Review
Corrections and comments
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Rapid development of diagnostic immunoassays against novel emerging or genetically modified pathogens in an emergency situation is dependent on the timely isolation of specific antibodies. Non-immune antibody phage display libraries are an efficient in vitro method for selecting monoclonal antibodies and hence ideal in these circumstances. Such libraries can be constructed from a variety of sources e.g. B cell cDNA or synthetically generated, and use a variety of antibody formats, typically scFv or Fab. However, antibody source and format can impact on the quality of antibodies generated and hence the effectiveness of this methodology for the timely production of antibodies. We have carried out a comparative screening of two antibody libraries, a semi-synthetic scFv library and a human-derived Fab library against the protective antigen toxin component of Bacillus anthracis and the epsilon toxin of Clostridium botulinum. We have shown that while the synthetic library produced a diverse collection of specific scFv-phage, these contained a high frequency of unnatural amber stops and glycosylation sites which limited their conversion to IgG, and also a high number which lost specificity when expressed as IgG. In contrast, these limitations were overcome by the use of a natural human library. Antibodies from both libraries could be used to develop sandwich ELISA assays with similar sensitivity. However, the ease and speed with which full-length IgG could be generated from the human-derived Fab library makes screening this type of library the preferable method for rapid antibody generation for diagnostic assay development.
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