ArticleScientific reports2017
The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 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
75 citing papers in PubMed, 113 citations in OpenAlex.
- Role of the C-terminal modules of Klebsiella phage KP32 receptor-binding protein gp38 in protein and phage functionality.PLoS pathogens · 2026Article
- Prophage: agent provocateur?Archives of microbiology · 2026Review
- Phage-Based Approaches to ChronicAntibiotics (Basel, Switzerland) · 2026Review
- Phage and endolysin-based inhibition ofFrontiers in cellular and infection microbiology · 2026Review
- Understanding phage Receptor-binding protein interaction with host surface receptor: the key for phage-Mediated detection and elimination of Pseudomonas aeruginosa.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Review
- Antivirulence Activity and Therapeutic Potential of JumboJournal of microbiology and biotechnology · 2025Article
- PDP-Miner: an AI/ML tool to detect prophage tail proteins with depolymerase domains across thousands of bacterial genomes.Bioinformatics (Oxford, England) · 2025Article
- Phage-encoded protein PavP modulates Pseudomonas aeruginosa virulence by dual inhibition of growth and pathogenic traits.Biology direct · 2025Article
- Antibiotic-resistant Acinetobacter baumannii can be killed by a combination of bacteriophages and complement.Medical microbiology and immunology · 2025Article
- The Ability of Bacteriophages to Reduce Biofilms Produced byAntibiotics (Basel, Switzerland) · 2025Article
- Klebsiella Lytic Phages InduceViruses · 2025Article
- Bacteriophage-derived depolymerase: a review on prospective antibacterial agents to combat Klebsiella pneumoniae.Archives of virology · 2025Review
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Pseudomonas aeruginosa as a model bacterium in antiphage defense research.FEMS microbiology reviews · 2025Review
- The complement system: A key player in the host response to infections.European journal of immunology · 2024Review
- Targeting Pseudomonas aeruginosa biofilm with an evolutionary trained bacteriophage cocktail exploiting phage resistance trade-offs.Nature communications · 2024Article
- Enterococcal quorum-controlled protease alters phage infection.bioRxiv : the preprint server for biology · 2024Article
- Article
- Review
- TSPDB: a curated resource of tailspike proteins with potential applications in phage research.Frontiers in big data · 2024Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 7 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas phage LKA1 of the subfamily Autographivirinae encodes a tailspike protein (LKA1gp49) which binds and cleaves B-band LPS (O-specific antigen, OSA) of Pseudomonas aeruginosa PAO1. The crystal structure of LKA1gp49 catalytic domain consists of a beta-helix, an insertion domain and a C-terminal discoidin-like domain. The putative substrate binding and processing site is located on the face of the beta-helix whereas the C-terminal domain is likely involved in carbohydrates binding. NMR spectroscopy and mass spectrometry analyses of degraded LPS (OSA) fragments show an O5 serotype-specific polysaccharide lyase specificity. LKA1gp49 reduces virulence in an in vivo Galleria mellonella infection model and sensitizes P. aeruginosa to serum complement activity. This enzyme causes biofilm degradation and does not affect the activity of ciprofloxacin and gentamicin. This is the first comprehensive report on LPS-degrading lyase derived from a Pseudomonas phage. Biological properties reveal a potential towards its applications in antimicrobial design and as a microbiological or biotechnological tool.
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.