ArticlePLoS pathogens2014
Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 2 of them syntheses that pooled it.
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
41 citing papers in PubMed, 2 syntheses or guidelines pooled it, 75 citations in OpenAlex.
- Antibacterial and antibiofilm activities of pyocins produced byFrontiers in microbiology · 2026Pooled it
- Tandem-repeat lectins: structural and functional insights.Glycobiology · 2024Pooled it
- L-type pyocins inhibit the BAM complex to kill without cell entry.Nature communications · 2026Article
- Mining Microbial Genomes for Anti-Pseudomonal Peptides: A Translational In Silico Framework.Current microbiology · 2026Article
- Lipopolysaccharide-targeting treatments for multidrug-resistantExpert opinion on therapeutic targets · 2026Review
- Genomic correlates of tailocin sensitivity in Pseudomonas syringae.G3 (Bethesda, Md.) · 2025Article
- Interactions between Lipopolysaccharide and Peptide Bacteriocin BacSp222 Influence Their Biological Activities.ACS infectious diseases · 2025Article
- Molecular and functional analysis of a putative pyocin S9, with endonuclease activity from P. chlororaphis subsp aurantiaca PB-St2.Archives of microbiology · 2025Article
- Pyocins and Beyond: Exploring the World of Bacteriocins in Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2025Review
- Outer membrane translocation of pyocins via the copper regulated TonB-dependent transporter CrtA.The Biochemical journal · 2023Article
- Recipient Cell Factors Influence Interbacterial Competition Mediated by Two Distinct Burkholderia dolosa Contact-Dependent Growth Inhibition Systems.Journal of bacteriology · 2022Article
- Biosynthesis of the Pseudomonas aeruginosa common polysaccharide antigen by D-Rhamnosyltransferases WbpX and WbpY.Glycoconjugate journal · 2022Article
- MvaT negatively regulates pyocin S5 expression inBiotechnology notes (Amsterdam, Netherlands) · 2022Article
- Antimicrobial Weapons of Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- Article
- Emerging Applications of Bacteriocins as Antimicrobials, Anticancer Drugs, and Modulators of The Gastrointestinal Microbiota.Polish journal of microbiology · 2021Review
- Chemical activation of Arabidopsis SnRK2.6 by pladienolide B.Plant signaling & behavior · 2021Article
- Engineering bacteriocin-mediated resistance against the plant pathogen Pseudomonas syringae.Plant biotechnology journal · 2020Article
- Pyocin S5 Import into Pseudomonas aeruginosa Reveals a Generic Mode of Bacteriocin Transport.mBio · 2020Article
- Bacteriocins Targeting Gram-Negative Phytopathogenic Bacteria: Plantibiotics of the Future.Frontiers in microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-specific killing activity. Here we show that pyocin L1, a novel member of this family from Pseudomonas aeruginosa, targets susceptible strains of this species through recognition of the common polysaccharide antigen (CPA) of P. aeruginosa lipopolysaccharide that is predominantly a homopolymer of D-rhamnose. Structural and biophysical analyses show that recognition of CPA occurs through the C-terminal carbohydrate-binding domain of pyocin L1 and that this interaction is a prerequisite for bactericidal activity. Further to this, we show that the previously described lectin-like bacteriocin putidacin L1 shows a similar carbohydrate-binding specificity, indicating that oligosaccharides containing D-rhamnose and not D-mannose, as was previously thought, are the physiologically relevant ligands for this group of bacteriocins. The widespread inclusion of d-rhamnose in the lipopolysaccharide of members of the genus Pseudomonas explains the unusual genus-specific activity of the lectin-like bacteriocins.
Indexed as
Identifiers
What OpenQuestion holds
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.