ArticleThe Journal of biological chemistry2013
Direct expression and validation of phage-selected peptide variants in mammalian cells.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- In vitro affinity maturation of broader and more-potent variants of the HIV-1-neutralizing antibody CAP256-VRC26.25.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A phage-displayed single-chain Fab library optimized for rapid production of single-chain IgGs.Protein science : a publication of the Protein Society · 2020Article
- Diverse pathways of escape from all well-characterized VRC01-class broadly neutralizing HIV-1 antibodies.PLoS pathogens · 2018Article
- eCD4-Ig promotes ADCC activity of sera from HIV-1-infected patients.PLoS pathogens · 2017Article
- Engineering antibody-like inhibitors to prevent and treat HIV-1 infection.Current opinion in HIV and AIDS · 2017Review
- pMINERVA: A donor-acceptor system for the in vivo recombineering of scFv into IgG molecules.Journal of immunological methods · 2016Article
- Article
- A double-mimetic peptide efficiently neutralizes HIV-1 by bridging the CD4- and coreceptor-binding sites of gp120.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Phage display is a key technology for the identification and maturation of high affinity peptides, antibodies, and other proteins. However, limitations of bacterial expression restrict the range and sensitivity of assays that can be used to evaluate phage-selected variants. To address this problem, selected genes are typically transferred to mammalian expression vectors, a major rate-limiting step in the iterative improvement of peptides and proteins. Here we describe a system that combines phage display and efficient mammalian expression in a single vector, pDQ1. This system permits immediate expression of phage-selected genes as IgG1-Fc fusions in mammalian cells, facilitating the rapid, sensitive characterization of a large number of library outputs for their biochemical and functional properties. We demonstrate the utility of this system by improving the ability of a CD4-mimetic peptide to bind the HIV-1 envelope glycoprotein and neutralize HIV-1 entry. We further improved the potency of the resulting peptide, CD4mim6, by limiting its ability to induce the CD4-bound conformation of the envelope glycoprotein. Thus, CD4mim6 and its variants can be used to investigate the properties of the HIV-1 envelope glycoprotein, and pDQ1 can accelerate the discovery of new peptides and proteins through phage display.
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What OpenQuestion holds
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.