ArticleThe Biochemical journal2016
Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- Designing the Next Generation of Endolysins: A Triple Strategy Integrating Bioinformatics Mining, Engineering Modification and Encapsulation Formulation.Probiotics and antimicrobial proteins · 2026Review
- Lipopolysaccharide-targeting treatments for multidrug-resistantExpert opinion on therapeutic targets · 2026Review
- Second-generation lysocins as therapeutics for treatingAntimicrobial agents and chemotherapy · 2025Article
- Interactions between Lipopolysaccharide and Peptide Bacteriocin BacSp222 Influence Their Biological Activities.ACS infectious diseases · 2025Article
- Lactic Acid Bacteria Bacteriocins: Safe and Effective Antimicrobial Agents.International journal of molecular sciences · 2025Review
- Pyocins and Beyond: Exploring the World of Bacteriocins in Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2025Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Assessment of bacteriocin production by clinical Pseudomonas aeruginosa isolates and their potential as therapeutic agents.Microbial cell factories · 2024Article
- Turbidimetric bioassays: A solution to antimicrobial activity detection in asymptomatic bacteriuria isolates against uropathogenic Escherichia coli.MicrobiologyOpen · 2024Article
- Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI.PNAS nexus · 2024Article
- Outer membrane translocation of pyocins via the copper regulated TonB-dependent transporter CrtA.The Biochemical journal · 2023Article
- The In Vivo and In Vitro Assessment of Pyocins in TreatingAntibiotics (Basel, Switzerland) · 2022Review
- Toxin import through the antibiotic efflux channel TolC.Nature communications · 2021Article
- Structural design principles for specific ultra-high affinity interactions between colicins/pyocins and immunity proteins.Scientific reports · 2021Article
- Review
- The Response ofInternational journal of molecular sciences · 2020Article
- Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.Journal of bacteriology · 2020Article
- Targeted Killing of Pseudomonas aeruginosa by Pyocin G Occurs via the Hemin Transporter Hur.Journal of molecular biology · 2020Article
- Multifunctional Acidocin 4356 CombatsApplied and environmental microbiology · 2020Article
- Pyocin S5 Import into Pseudomonas aeruginosa Reveals a Generic Mode of Bacteriocin Transport.mBio · 2020Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Increasing rates of antibiotic resistance among Gram-negative pathogens such as Pseudomonas aeruginosa means alternative approaches to antibiotic development are urgently required. Pyocins, produced by P. aeruginosa for intraspecies competition, are highly potent protein antibiotics known to actively translocate across the outer membrane of P. aeruginosa. Understanding and exploiting the mechanisms by which pyocins target, penetrate and kill P. aeruginosa is a promising approach to antibiotic development. In this work we show the therapeutic potential of a newly identified tRNase pyocin, pyocin SD2, by demonstrating its activity in vivo in a murine model of P. aeruginosa lung infection. In addition, we propose a mechanism of cell targeting and translocation for pyocin SD2 across the P. aeruginosa outer membrane. Pyocin SD2 is concentrated at the cell surface, via binding to the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide (LPS), from where it can efficiently locate its outer membrane receptor FpvAI. This strategy of utilizing both the CPA and a protein receptor for cell targeting is common among pyocins as we show that pyocins S2, S5 and SD3 also bind to the CPA. Additional data indicate a key role for an unstructured N-terminal region of pyocin SD2 in the subsequent translocation of the pyocin into the cell. These results greatly improve our understanding of how pyocins target and translocate across the outer membrane of P. aeruginosa. This knowledge could be useful for the development of novel anti-pseudomonal therapeutics and will also support the development of pyocin SD2 as a therapeutic in its own right.
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Registered trials
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