ReviewJournal of molecular biology2019
The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents.
Review in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 75 citations in OpenAlex.
- Current Status and Future Challenges in the Use of Bacteriocins to Modulate Ruminant Gut Microbiota.Probiotics and antimicrobial proteins · 2026Review
- Functional organization and regulatory logic of theApplied and environmental microbiology · 2026Review
- Thyme, Oregano, and Cinnamon Essential Oils: Investigating Their Molecular Mechanism of Action for the Treatment of Bacteria-Induced Cystitis.ACS omega · 2026Article
- Heterologous expression and functional characterization of novel microcin B17 congeners from environmental Pseudomonas isolates.Applied microbiology and biotechnology · 2026Article
- Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V.Communications biology · 2025Article
- A chlorinated diketopiperazine antibiotic targetsAntimicrobial agents and chemotherapy · 2025Article
- A dual expression plasmid with Microcin B17 compatible with both prokaryotic and mammalian systems.MethodsX · 2025Article
- Antimicrobial peptides and proteins against drug-resistant pathogens.Cell surface (Amsterdam, Netherlands) · 2024Review
- The role of prokaryotic argonautes in resistance to type II topoisomerases poison ciprofloxacin.Biochemical Society transactions · 2024Review
- Mycobacterium smegmatis MfpC is a GEF that regulates mfpA translationally to alter the fluoroquinolone efficacy.Communications biology · 2024Article
- Enterolyin S, a Polythiazole-containing Hemolytic Peptide from Enterococcus caccae.Chembiochem : a European journal of chemical biology · 2024Article
- Complete nucleotide sequence and comparative genomic analysis of microcin B17 plasmid pMccB17.MicrobiologyOpen · 2024Article
- Exploring the genetic basis of natural resistance to microcins.Microbial genomics · 2024Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Biochemistry, Mechanistic Intricacies, and Therapeutic Potential of Antimicrobial Peptides: An Alternative to Traditional Antibiotics.Current medicinal chemistry · 2024Review
- Comprehensive Analysis of Bacteriocins Produced by the Hypermucoviscous Klebsiella pneumoniae Species Complex.Microbiology spectrum · 2023Article
- Antiproliferative activity of antimicrobial peptides and bioactive compounds from the mangroveFrontiers in microbiology · 2023Article
- Review
- Antimicrobial Mechanisms and Clinical Application Prospects of Antimicrobial Peptides.Molecules (Basel, Switzerland) · 2022Review
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Microcin B17 (MccB17) is an antibacterial peptide produced by strains of Escherichia coli harboring the plasmid-borne mccB17 operon. MccB17 possesses many notable features. It is able to stabilize the transient DNA gyrase-DNA cleavage complex, a very efficient mode of action shared with the highly successful fluoroquinolone drugs. MccB17 stabilizes this complex by a distinct mechanism making it potentially valuable in the fight against bacterial antibiotic resistance. MccB17 was the first compound discovered from the thiazole/oxazole-modified microcins family and the linear azole-containing peptides; these ribosomal peptides are post-translationally modified to convert serine and cysteine residues into oxazole and thiazole rings. These chemical moieties are found in many other bioactive compounds like the vitamin thiamine, the anti-cancer drug bleomycin, the antibacterial sulfathiazole and the antiviral nitazoxanide. Therefore, the biosynthetic machinery that produces these azole rings is noteworthy as a general method to create bioactive compounds. Our knowledge of MccB17 now extends to many aspects of antibacterial-bacteria interactions: production, transport, interaction with its target, and resistance mechanisms; this knowledge has wide potential applicability. After a long time with limited progress on MccB17, recent publications have addressed critical aspects of MccB17 biosynthesis as well as an explosion in the discovery of new related compounds in the thiazole/oxazole-modified microcins/linear azole-containing peptides family. It is therefore timely to summarize the evidence gathered over more than 40 years about this still enigmatic molecule and place it in the wider context of antibacterials.
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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.