ArticleProtein science : a publication of the Protein Society2006
Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Bacterial Display of Genetically Encoded Macrocyclic Peptide Libraries Using Cysteine-Reactive Unnatural Amino Acids.ACS chemical biology · 2026Article
- Engineering of Surface Display Systems inBiotech (Basel (Switzerland)) · 2026Article
- A proteome-wide biochemical screen defines binding determinants of the core autophagy protein LC3B.bioRxiv : the preprint server for biology · 2026Article
- Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Synergistic collaboration between AMPs and non-direct antimicrobial cationic peptides.Nature communications · 2024Article
- Phage-encoded bismuth bicycles enable instant access to targeted bioactive peptides.Communications chemistry · 2024Article
- Fluorescent Labeling of Outer Membrane Proteins Using the SpyCatcher-SpyTag System.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Artificial surface labelling of Escherichia coli with StrepTagII antigen to study how monoclonal antibodies drive complement-mediated killing.Scientific reports · 2023Article
- Embracing enzyme promiscuity with activity-based compressed biosensing.Cell reports methods · 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
- The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) ofFrontiers in molecular biosciences · 2022Article
- Conditional PD-1/PD-L1 Probody Therapeutics Induce Comparable Antitumor Immunity but Reduced Systemic Toxicity Compared with Traditional Anti-PD-1/PD-L1 Agents.Cancer immunology research · 2021Article
- Novel Ex Vivo Zymography Approach for Assessment of Protease Activity in Tissues with Activatable Antibodies.Pharmaceutics · 2021Article
- Directed Evolution Using Stabilized Bacterial Peptide Display.Journal of the American Chemical Society · 2020Article
- The next generation of biopanning: next gen sequencing improves analysis of bacterial display libraries.BMC biotechnology · 2019Article
- FimH-based display of functional eukaryotic proteins on bacteria surfaces.Scientific reports · 2019Article
- A bacterial display system for effective selection of protein-biotin ligase BirA variants with novel peptide specificity.Scientific reports · 2019Article
- Article
- Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates.Journal of visualized experiments : JoVE · 2017Article
- Escherichia coli surface display for the selection of nanobodies.Microbial biotechnology · 2017Review
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5 authors.
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Abstract
A bacterial display methodology was developed for N- and C-terminal display and demonstrated to enable rapid screening of very large peptide libraries with high precision and efficiency. To overcome limitations of insertional fusion display libraries, a new scaffold was developed through circular permutation of the Escherichia coli outer membrane protein OmpX that presents both N and C termini on the external cell surface. Circularly permuted OmpX (CPX) display was directly compared to insertional fusion display by screening comparable peptide libraries in each format using magnetic and fluorescence activated cell sorting. CPX display enabled in situ measurement of dissociation rate constants with improved accuracy and, consequently, improved affinity discrimination during screening and ranking of isolated clones. Using streptavidin as a model target, bacterial display yielded the well-characterized HP(Q)/(M) motif obtained previously using several alternative peptide display systems, as well as three additional motifs (L(I)/(V) CQNVCY, CGWMY(F)/(Y)xEC, ERCWYVMHWPCNA). Using CPX display, a very high affinity streptavidin-binding peptide was isolated having a dissociation rate constant k(off) = 0.002sec(-1) even after grafting to the C terminus of an unrelated protein. Comparison of individual clones obtained from insertional fusion and terminal fusion libraries suggests that the N-terminal display yields sequences with greater diversity, affinity, and modularity. CPX bacterial display thus provides a highly effective method for screening peptide libraries to rapidly generate ligands with high affinity and specificity.
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