ArticleApplied and environmental microbiology2022
Structural Basis of Pore Formation in the Mannose Phosphotransferase System by Pediocin PA-1.
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 48 citations in OpenAlex.
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- Uncovering how selected potent bacteriocins reshape the broiler chicken gut microbiome in a PolyFermS continuous in vitro model.Journal of animal science and biotechnology · 2026Article
- Genome-guided antimicrobial potential of Bacillus stercoris from coastal sand with activity against multidrug-resistant bacteria, including MRSA.International microbiology : the official journal of the Spanish Society for Microbiology · 2026Article
- A trimeric architecture reveals the glucitol PTS transporter as a distinct superfamily.Communications biology · 2026Article
- Structural basis for the extended-spectrum antimicrobial activity of Garvieacin Q.Applied and environmental microbiology · 2026Article
- Prophylactic efficacy of probiotics and their metabolites against Staphylococcus epidermidis.BMC microbiology · 2025Article
- Solution Structure of the Broad-Spectrum Bacteriocin Garvicin Q.International journal of molecular sciences · 2025Article
- Uncovering the arsenal of class II bacteriocins in salivarius streptococci.Communications biology · 2024Article
- Biopreservation strategies using bacteriocins to control meat spoilage and foodborne outbreaks.Italian journal of food safety · 2024Review
- Acidocin A and Acidocin 8912 Belong to a Distinct Subfamily of Class II Bacteriocins with a Broad Spectrum of Antimicrobial Activity.International journal of molecular sciences · 2024Article
- Article
- Bacteriocin diversity, function, discovery and application as antimicrobials.Nature reviews. Microbiology · 2024Review
- Bacteriocins in Cancer Treatment: Mechanisms and Clinical Potentials.Biomolecules · 2024Review
- Beyond Conventional Meat Preservation: Saddling the Control of Bacteriocin and Lactic Acid Bacteria for Clean Label and Functional Meat Products.Applied biochemistry and biotechnology · 2024Review
- The Progress of the Biotechnological Production of Class IIa Bacteriocins in Various Cell Factories and Its Future Challenges.International journal of molecular sciences · 2024Review
- Bacteriocins: potentials and prospects in health and agrifood systems.Archives of microbiology · 2024Review
- Tertiary Plasticity Drives the Efficiency of Enterocin 7B Interactions with Lipid Membranes.The journal of physical chemistry. B · 2024Article
- Antimicrobial Activity of Synthetic Enterocins A, B, P, SEK4, and L50, Alone and in Combinations, againstInternational journal of molecular sciences · 2024Article
- Article
- High-throughput detection of potential bacteriocin producers in a large strain library using live fluorescent biosensors.Frontiers in bioengineering and biotechnology · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or class IIa) bacteriocins (PLBs) exhibit antibacterial activity against several Gram-positive bacterial strains by forming pores in the cytoplasmic membrane of target cells with a specific receptor, the mannose phosphotransferase system (man-PTS). In this study, we report the cryo-electron microscopy structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1, the first and most extensively studied representative PLB, at resolutions of 3.12 and 2.45 Å, respectively. The structures revealed that the binding of pediocin PA-1 opens the Core domain of man-PTS away from its Vmotif domain, creating a pore through the cytoplasmic membranes of target cells. During this process, the N-terminal β-sheet region of pediocin PA-1 can specifically attach to the extracellular surface of the man-PTS Core domain, whereas the C-terminal half penetrates the membrane and cracks the man-PTS like a wedge. Thus, our findings shed light on a design of novel PLBs that can kill the target pathogenic bacteria.
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