ArticleProceedings of the National Academy of Sciences of the United States of America2010
Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 89 citations in OpenAlex.
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.PNAS nexus · 2024Article
- Interaction of Tryptophan- and Arginine-Rich Antimicrobial Peptide withInternational journal of molecular sciences · 2023Article
- Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope.PLoS genetics · 2023Article
- Colicin E2 expression in Escherichia coli biofilms: Induction and regulation revisited.Current research in microbial sciences · 2022Article
- Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF.The EMBO journal · 2021Article
- Article
- Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer.Journal of the American Chemical Society · 2020Article
- Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N intoThe Journal of biological chemistry · 2020Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins.Nature methods · 2020Article
- The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium.Scientific reports · 2019Article
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Directional Porin Binding of Intrinsically Disordered Protein Sequences Promotes Colicin Epitope Display in the Bacterial Periplasm.Biochemistry · 2018Article
- Native Desorption Electrospray Ionization Liberates Soluble and Membrane Protein Complexes from Surfaces.Angewandte Chemie (International ed. in English) · 2017Article
- Exploitation of an iron transporter for bacterial protein antibiotic import.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- Diversity and distribution of nuclease bacteriocins in bacterial genomes revealed using Hidden Markov Models.PLoS computational biology · 2017Article
- The Colicin E1 TolC Box: Identification of a Domain Required for Colicin E1 Cytotoxicity and TolC Binding.Journal of bacteriology · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The porins OmpF and OmpC are trimeric β-barrel proteins with narrow channels running through each monomer that exclude molecules > 600 Da while mediating the passive diffusion of small nutrients and metabolites across the Gram-negative outer membrane (OM). Here, we elucidate the mechanism by which an entire soluble protein domain (> 6 kDa) is delivered through the lumen of such porins. Following high-affinity binding to the vitamin B(12) receptor in Escherichia coli, the bacteriocin ColE9 recruits OmpF or OmpC using an 83-residue intrinsically unstructured translocation domain (IUTD) to deliver a 16-residue TolB-binding epitope (TBE) in the center of the IUTD to the periplasm where it triggers toxin entry. We demonstrate that the IUTD houses two OmpF-binding sites, OBS1 (residues 2-18) and OBS2 (residues 54-63), which flank the TBE and bind with K(d)s of 2 and 24 μM, respectively, at pH 6.5 and 25 ºC. We show the two OBSs share the same binding site on OmpF and that the colicin must house at least one of them for antibiotic activity. Finally, we report the structure of the OmpF-OBS1 complex that shows the colicin bound within the porin lumen spanning the membrane bilayer. Our study explains how colicins exploit porins to deliver epitope signals to the bacterial periplasm and, more broadly, how the inherent flexibility and narrow cross-sectional area of an IUP domain can endow it with the ability to traverse a biological membrane via the constricted lumen of a β-barrel membrane protein.
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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.