ArticleProtein engineering, design & selection : PEDS2008
Directed evolution of a biterminal bacterial display scaffold enhances the display of diverse peptides.
Article in Protein engineering, design & selection : PEDS, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
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- Bacterial surface display enables lysis-independent joint host-pathogen single-cell profiling.bioRxiv : the preprint server for biology · 2026Article
- Context-dependent peptide recognition shapes tyrosine kinase substrate specificity beyond consensus motifs.bioRxiv : the preprint server for biology · 2026Article
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- Profiling tyrosine kinase substrate recognition using bacterial peptide display and deep sequencing.bioRxiv : the preprint server for biology · 2025Article
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- Identification of pancreatic cancer-specific protease substrates for protease-dependent targeted delivery.Oncogenesis · 2024Article
- Repurposing Copper(II)/THPTA as A Bioorthogonal Catalyst for Thiazolidine Bond Cleavage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Elaboration of the Homer1 recognition landscape reveals incomplete divergence of paralogous EVH1 domains.Protein science : a publication of the Protein Society · 2024Article
- Elaboration of the Homer1 Recognition Landscape Reveals Incomplete Divergence of Paralogous EVH1 Domains.bioRxiv : the preprint server for biology · 2024Article
- An Adenosylcobalamin Specific Whole-Cell Biosensor.Advanced healthcare materials · 2023Article
- Scalable Production of Peptides for Enhanced Struvite Formation via Expression on the Surface of Genetically Engineered Microbes.ACS materials Au · 2023Article
- Rapid Evaluation of Staple Placement in Stabilized α Helices Using Bacterial Surface Display.ACS chemical biology · 2023Article
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- Identification of Microorganisms that Bind Specifically to Target Materials of Interest Using a Magnetophoretic Microfluidic Platform.ACS applied materials & interfaces · 2023Article
- Molecular determinants of TRAF6 binding specificity suggest that native interaction partners are not optimized for affinity.Protein science : a publication of the Protein Society · 2022Article
- Blue Light Signaling Regulates Escherichia coli W1688 Biofilm Formation and l-Threonine Production.Microbiology spectrum · 2022Article
- Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the prehairpin intermediate of the spike protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Saturation mutagenesis of a predicted ancestral Syk-family kinase.Protein science : a publication of the Protein Society · 2022Article
- Prediction of protein-ligand binding affinity from sequencing data with interpretable machine learning.Nature biotechnology · 2022Article
Corrections and comments
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cell-surface display systems coupled with quantitative screening methods offer the potential to expand protein engineering capabilities. To more fully exploit this potential, a unique bacterial surface display scaffold was engineered to display peptides more efficiently from the surface exposed C- and N-termini of a circularly permuted outer membrane protein. Using directed evolution, efficient membrane localization of a circularly permuted OmpX (CPX) display scaffold was rescued, thereby improving the presentation of diverse passenger peptides on the cell surface. Random and targeted mutagenesis directed towards linkers joining the native N- and C-termini of OmpX coupled with screening by FACS yielded an enhanced CPX (eCPX) variant which localized to the outer membrane as efficiently as the non-permuted parent. Interestingly, enhancing substitutions coincided with a C-terminal motif conserved in outer membrane proteins. Surface localization of various passenger peptides and mini-proteins was expedited using eCPX relative to that achieved with the parent scaffold. The new variant also permitted simultaneous display and labeling of distinct peptides on structurally adjacent C- and N-termini, thus enabling display level normalization during library screening and the display of bidentate or dimeric peptides. Consequently, the evolved scaffold, eCPX, expands the range of applications for bacterial display. Finally, this approach provides a route to improve the performance of cell-surface display vectors for protein engineering and design.
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