ArticleJournal of bacteriology2006
Bactericidal activity of both secreted and nonsecreted microcin E492 requires the mannose permease.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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.
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Who cites it
33 citing papers in PubMed, 67 citations in OpenAlex.
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- Novel class IIb microcins show activity against Gram-negative ESKAPE and plant pathogens.eLife · 2024Article
- Contact-dependent growth inhibition (CDI) systems deploy a large family of polymorphic ionophoric toxins for inter-bacterial competition.PLoS genetics · 2024Article
- TheApplied and environmental microbiology · 2024Article
- Immunomodulation, Bioavailability and Safety of Bacteriocins.Life (Basel, Switzerland) · 2023Review
- Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
- Mechanisms of action of ribosomally synthesized and posttranslationally modified peptides (RiPPs).Journal of industrial microbiology & biotechnology · 2021Review
- Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin.Cell discovery · 2021Article
- Bacteriocins as a new generation of antimicrobials: toxicity aspects and regulations.FEMS microbiology reviews · 2021Review
- Bacteriocins: Potential for Human Health.Oxidative medicine and cellular longevity · 2021Review
- Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020Review
- The manifold roles of microbial ribosomal peptide-based natural products in physiology and ecology.The Journal of biological chemistry · 2020Review
- Siderophore-Microcins inFrontiers in cellular and infection microbiology · 2020Review
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Microcin PDI Inhibits Antibiotic-Resistant Strains of Escherichia coli andApplied and environmental microbiology · 2019Article
- Mechanisms of Resistance to the Contact-Dependent Bacteriocin CdzC/D inJournal of bacteriology · 2019Article
- Microcins inFrontiers in microbiology · 2019Review
- Bioinspired Designs, Molecular Premise and Tools for Evaluating the Ecological Importance of Antimicrobial Peptides.Pharmaceuticals (Basel, Switzerland) · 2018Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microcin E492 (MccE492) is a bactericidal protein secreted by Klebsiella pneumoniae that is active against various species of Enterobacteriaceae. Interaction of MccE492 with target cells leads to the depolarization and permeabilization of their inner membranes. Several MccE492-specific proteins are required for the maturation and secretion of active MccE492. Surprisingly, the expression of only MceA, the polypeptide backbone of MccE492, is shown here to be toxic by itself. We refer to this phenomenon as endogenous MceA bactericidal activity to differentiate it from the action of extracellularly secreted MccE492. The toxicity of endogenous MceA is enhanced by an efficient targeting to the inner membrane. However, a periplasmic intermediate state is not required for MceA toxicity. Indeed, endogenous MceA remains fully active when it is fused to thioredoxin-1, a fast-folding protein that promotes retention of the C terminus of MceA in the cytoplasm. The C-terminal domain of MccE492 is required only for delivery from the extracellular environment to the periplasm, and it is not required for inner membrane damage. A common component is absolutely essential for the bactericidal activity of both endogenous MceA and extracellular MccE492. Indeed, toxicity is strictly dependent on the presence of ManYZ, an inner membrane protein complex involved in mannose uptake. Based on these findings, we propose a new model for cell entry, inner membrane insertion, and toxic activity of MccE492.
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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.