ArticleJournal of molecular biology2012
Engineering antibody fitness and function using membrane-anchored display of correctly folded proteins.
Article in Journal of molecular biology, 2012. 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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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
13 citing papers in PubMed.
- An Engineered Outer Membrane-DefectiveJournal of microbiology and biotechnology · 2022Article
- A human apolipoprotein L with detergent-like activity kills intracellular pathogens.Science (New York, N.Y.) · 2021Article
- Characterization of a novel method for the production of single-span membrane proteins in Escherichia coli.Biotechnology and bioengineering · 2019Article
- Efficient affinity maturation of antibody variable domains requires co-selection of compensatory mutations to maintain thermodynamic stability.Scientific reports · 2017Article
- Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments.Journal of visualized experiments : JoVE · 2016Article
- An Intrabody Drug (rAAV6-INT41) Reduces the Binding of N-Terminal Huntingtin Fragment(s) to DNA to Basal Levels in PC12 Cells and Delays Cognitive Loss in the R6/2 Animal Model.Journal of neurodegenerative diseases · 2016Article
- Repurposing a bacterial quality control mechanism to enhance enzyme production in living cells.Journal of molecular biology · 2015Article
- Review
- An engineered genetic selection for ternary protein complexes inspired by a natural three-component hitchhiker mechanism.Scientific reports · 2014Article
- Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selection.Protein engineering, design & selection : PEDS · 2014Article
- Ubiquibodies, synthetic E3 ubiquitin ligases endowed with unnatural substrate specificity for targeted protein silencing.The Journal of biological chemistry · 2014Article
- Directed evolution of human heavy chain variable domain (VH) using in vivo protein fitness filter.PloS one · 2014Article
- Hapten mediated display and pairing of recombinant antibodies accelerates assay assembly for biothreat countermeasures.Scientific reports · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
A hallmark of the bacterial twin-arginine translocation (Tat) pathway is its ability to export folded proteins. Here, we discovered that overexpressed Tat substrate proteins form two distinct, long-lived translocation intermediates that are readily detected by immunolabeling methods. Formation of the early translocation intermediate Ti-1, which exposes the N- and C-termini to the cytoplasm, did not require an intact Tat translocase, a functional Tat signal peptide, or a correctly folded substrate. In contrast, formation of the later translocation intermediate, Ti-2, which exhibits a bitopic topology with the N-terminus in the cytoplasm and C-terminus in the periplasm, was much more particular, requiring an intact translocase, a functional signal peptide, and a correctly folded substrate protein. The ability to directly detect Ti-2 intermediates was subsequently exploited for a new protein engineering technology called MAD-TRAP (membrane-anchored display for Tat-based recognition of associating proteins). Through the use of just two rounds of mutagenesis and screening with MAD-TRAP, the intracellular folding and antigen-binding activity of a human single-chain antibody fragment were simultaneously improved. This approach has several advantages for library screening, including the unique involvement of the Tat folding quality control mechanism that ensures only native-like proteins are displayed, thus eliminating poorly folded sequences from the screening process.
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Registered trials
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