ArticleAntimicrobial agents and chemotherapy2007
Modular structure of microcin H47 and colicin V.
Article in Antimicrobial agents and chemotherapy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
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- Prevalence and activity of class II microcins inApplied and environmental microbiology · 2026Article
- Refactored genetic parts for modular assembly of the E. coli MccV type I secretion system used to screen class II microcin candidates from plant-associated bacteria.BMC biotechnology · 2026Article
- Antibacterial microcins self-assemble to promote biofilm formation in Acinetobacter baumannii.Cell reports · 2026Article
- Selective cytotoxicity of microcin H47 against MDA-MB-231 breast cancer cells: an antimicrobial peptide with therapeutic potential.Archives of microbiology · 2026Article
- Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V.Communications biology · 2025Article
- Antibacterial microcins are ubiquitous and functionally diverse across bacterial communities.Nature communications · 2025Article
- Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli.Microbial cell factories · 2024Article
- Class IIb Microcin MccM Interferes with Oxidative Phosphorylation inACS chemical biology · 2024Article
- Export of Diverse and Bioactive Small Proteins through a Type I Secretion System.Applied and environmental microbiology · 2023Article
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
- Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin.Cell discovery · 2021Article
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Prevalence of Virulence Genes and Their Association with Antimicrobial Resistance Among PathogenicInfection and drug resistance · 2020Article
- Hybrids made from antimicrobial peptides with different mechanisms of action show enhanced membrane permeabilization.Biochimica et biophysica acta. Biomembranes · 2019Article
- Bacteriocin Occurrence and Activity inToxins · 2019Article
- Two New Plasmid Post-segregational Killing Mechanisms for the Implementation of Synthetic Gene Networks in Escherichia coli.iScience · 2019Article
- Microcins inFrontiers in microbiology · 2019Review
- Engineered E. coli Nissle 1917 for the reduction of vancomycin-resistantBioengineering & translational medicine · 2018Article
- pMPES: A Modular Peptide Expression System for the Delivery of Antimicrobial Peptides to the Site of Gastrointestinal Infections Using Probiotics.Pharmaceuticals (Basel, Switzerland) · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microcins are gene-encoded peptide antibiotics produced by enterobacteria that act on strains of gram-negative bacteria. In this work, we concentrated on higher-molecular-mass microcins, i.e., those possessing 60 or more amino acids. They can be subdivided into unmodified and posttranslationally modified peptides. In both cases, they exhibit conserved C-terminal sequences that appear to be characteristic of each subgroup. In the hypothesis that these sequences could correspond to domains, gene fusions between the activity genes for the unmodified microcin colicin V and the modified microcin H47 were constructed. These two microcins differ in their mode of synthesis, uptake, target, and specific immunity. Through this experimental approach, chimeric peptides with exchanged C-terminal sequences were encoded. Cells carrying the fusions in different genetic contexts were then assayed for antibiotic production. Many of them produced antibiotic activities with recombinant properties: the toxicity of one microcin and the mode of uptake of the other. The results led to the identification of a modular structure of colicin V and microcin H47, with the recognition of two domains in their peptide chains: a toxic N-terminal domain and an uptake C-terminal domain. This modular design would be shared by other microcins from each subgroup.
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Registered trials
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.