ArticleMolecular microbiology2014
The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 44 citations in OpenAlex.
- Purification of Bacterial Lipopolysaccharide, and How to Study Its Interactions with Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Interactions between Lipopolysaccharide and Peptide Bacteriocin BacSp222 Influence Their Biological Activities.ACS infectious diseases · 2025Article
- Lipopolysaccharide nanoparticles: A biomimetic platform to study bacterial surface.Biophysical journal · 2025Article
- Interaction of Tryptophan- and Arginine-Rich Antimicrobial Peptide withInternational journal of molecular sciences · 2023Article
- Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.The Journal of membrane biology · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Interactions of polymyxin B with lipopolysaccharide-containing membranes.Faraday discussions · 2021Article
- Review
- Resurfacing receptor binding domain of Colicin N to enhance its cytotoxic effect on human lung cancer cells.Computational and structural biotechnology journal · 2021Article
- 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
- Review
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Acquisition of MACPF domain-encoding genes is the main contributor to LPS glycan diversity in gut Bacteroides species.The ISME journal · 2018Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- The therapeutic potential of bacteriocins as protein antibiotics.Emerging topics in life sciences · 2017Article
- Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.The Biochemical journal · 2016Article
- The Effect of Lipopolysaccharide Core Oligosaccharide Size on the Electrostatic Binding of Antimicrobial Proteins to Models of the Gram Negative Bacterial Outer Membrane.Langmuir : the ACS journal of surfaces and colloids · 2016Article
- Dynamics and Interactions of OmpF and LPS: Influence on Pore Accessibility and Ion Permeability.Biophysical journal · 2016Article
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9 authors at 3 institutions in 2 countries.
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Abstract
Colicins are a diverse family of large antibacterial protein toxins, secreted by and active against Escherichia coli and must cross their target cell's outer membrane barrier to kill. To achieve this, most colicins require an abundant porin (e.g. OmpF) plus a low-copy-number, high-affinity, outer membrane protein receptor (e.g. BtuB). Recently, genetic screens have suggested that colicin N (ColN), which has no high-affinity receptor, targets highly abundant lipopolysaccharide (LPS) instead. Here we reveal the details of this interaction and demonstrate that the ColN receptor-binding domain (ColN-R) binds to a specific region of LPS close to the membrane surface. Data from in vitro studies using calorimetry and both liquid- and solid-state NMR reveal the interactions behind the in vivo requirement for a defined oligosaccharide region of LPS. Delipidated LPS (LPS(Δ) (LIPID) ) shows weaker binding; and thus full affinity requires the lipid component. The site of LPS binding means that ColN will preferably bind at the interface and thus position itself close to the surface of its translocon component, OmpF. ColN is, currently, unique among colicins in requiring LPS and, combined with previous data, this implies that the ColN translocon is distinct from those of other known colicins.
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