ArticleProtein science : a publication of the Protein Society2015
Selection of recombinant anti-SH3 domain antibodies by high-throughput phage display.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Review
- A novel nanobody-based HER2-targeting antibody exhibits potent synergistic antitumor efficacy in trastuzumab-resistant cancer cells.Frontiers in immunology · 2023Article
- Revisiting the phosphotyrosine binding pocket of Fyn SH2 domain led to the identification of novel SH2 superbinders.Protein science : a publication of the Protein Society · 2021Article
- A High-Throughput Platform for the Generation of Synthetic Ab Clones by Single-Strand Site-Directed Mutagenesis.Molecular biotechnology · 2019Article
- Highly multiplexed and quantitative cell-surface protein profiling using genetically barcoded antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A panel of synthetic antibodies that selectively recognize and antagonize members of the interferon alpha family.Protein engineering, design & selection : PEDS · 2017Article
- Phage-Enabled Nanomedicine: From Probes to Therapeutics in Precision Medicine.Angewandte Chemie (International ed. in English) · 2017Review
- A high-throughput pipeline for the production of synthetic antibodies for analysis of ribonucleoprotein complexes.RNA (New York, N.Y.) · 2016Article
- Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Antibodies are indispensable tools in biochemical research and play an expanding role as therapeutics. While hybridoma technology is the dominant method for antibody production, phage display is an emerging technology. Here, we developed and employed a high-throughput pipeline that enables selection of antibodies against hundreds of antigens in parallel. Binding selections using a phage-displayed synthetic antigen-binding fragment (Fab) library against 110 human SH3 domains yielded hundreds of Fabs targeting 58 antigens. Affinity assays demonstrated that representative Fabs bind tightly and specifically to their targets. Furthermore, we developed an efficient affinity maturation strategy adaptable to high-throughput, which increased affinity dramatically but did not compromise specificity. Finally, we tested Fabs in common cell biology applications and confirmed recognition of the full-length antigen in immunoprecipitation, immunoblotting and immunofluorescence assays. In summary, we have established a rapid and robust high-throughput methodology that can be applied to generate highly functional and renewable antibodies targeting protein domains on a proteome-wide scale.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.