ArticleJournal of molecular biology2007
A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selection.Protein engineering, design & selection : PEDS · 2014Article
- Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.The Journal of biological chemistry · 2014Article
- Directed evolution of human heavy chain variable domain (VH) using in vivo protein fitness filter.PloS one · 2014Article
- Affinity maturation of an anti-V antigen IgG expressed in situ through adenovirus gene delivery confers enhanced protection against Yersinia pestis challenge.Gene therapy · 2010Article
- TAT-pathway-dependent lipoproteins as a niche-based adaptation in prokaryotes.Journal of molecular evolution · 2010Article
- Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.PloS one · 2010Article
- Mining mammalian genomes for folding competent proteins using Tat-dependent genetic selection in Escherichia coli.Protein science : a publication of the Protein Society · 2009Article
- Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Microbial cell factories · 2009Article
- Engineering antibody fragments to fold in the absence of disulfide bonds.Protein science : a publication of the Protein Society · 2009Article
- Efficient isolation of soluble intracellular single-chain antibodies using the twin-arginine translocation machinery.Journal of molecular biology · 2009Article
- Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli.Microbial biotechnology · 2008Article
- Synthetic antibody libraries focused towards peptide ligands.Journal of molecular biology · 2008Article
- Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Proteins destined for export across the cytoplasmic membrane via the post-translational Sec-dependent route have to be maintained in a largely unfolded state within the cytoplasm. In sharp contrast, only proteins that have folded into a native-like state within the cytoplasm are competent for export via the twin arginine translocation (Tat) pathway. Proteins that contain disulfide bonds, such as scFv antibody fragments, can be translocated via Tat only when expressed in Escherichia coli trxB gor mutant strains having an oxidizing cytoplasm. However, export is poor with the majority of the protein accumulating in the cytoplasm and only a fraction exported to the periplasmic space. Using a high throughput fluorescence screen, we isolated a mutant of the anti-digoxin 26-10 scFv from a large library of random mutants that is exported with a higher yield into the periplasm. In vitro refolding experiments revealed that the mutant scFv exhibits a 250% increase in the rate constant of the critical second phase of folding. This result suggests that Tat export competence is related to the protein folding rate and could be exploited for the isolation of faster folding protein mutants.
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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.