ArticleInfection and immunity1993
Cloning, expression, and mutagenesis of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: a potential staphylococcal virulence factor.
Article in Infection and immunity, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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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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.
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Who cites it
29 citing papers in PubMed, 63 citations in OpenAlex.
- "Just the Best Ones" combination: a new strategy for multi-epitope vaccine candidate based on immunoinformatics analysis to induce protective immunity against MRSA infection.Microbiology spectrum · 2026Article
- Protection of Mice Vaccinated with a New B Cell and T Cell Epitopes Cocktail from Staphylococcus aureus Challenge in Skin Infection Model.Current microbiology · 2025Article
- ImmobilizedFrontiers in bioengineering and biotechnology · 2025Article
- Phospholipase C: underrated players in microbial infections.Frontiers in cellular and infection microbiology · 2023Review
- PKCα Is Recruited toFrontiers in immunology · 2021Article
- Phosphatidylinositol-specific phospholipase C enhances epidermal penetration by Staphylococcus aureus.Scientific reports · 2020Article
- Comparative Genomics of Plasmid-BearingFrontiers in microbiology · 2020Article
- Review
- Prevalence of Antibiotic and Heavy Metal Resistance Determinants and Virulence-Related Genetic Elements in Plasmids ofFrontiers in microbiology · 2019Article
- The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.Toxins · 2017Review
- Phosphatidylinositol-specific phospholipase C contributes to survival of Staphylococcus aureus USA300 in human blood and neutrophils.Infection and immunity · 2014Article
- Development of a novel selective and differential medium for the isolation of Listeria monocytogenes.Applied and environmental microbiology · 2014Article
- Characterization of Plp, a phosphatidylcholine-specific phospholipase and hemolysin of Vibrio anguillarum.BMC microbiology · 2013Article
- The cation-π box is a specific phosphatidylcholine membrane targeting motif.The Journal of biological chemistry · 2013Article
- Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding?Biophysical journal · 2013Article
- Competition between anion binding and dimerization modulates Staphylococcus aureus phosphatidylinositol-specific phospholipase C enzymatic activity.The Journal of biological chemistry · 2012Article
- Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop.Biochemistry · 2012Article
- Peptide signaling in the staphylococci.Chemical reviews · 2011Review
- Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding.Biochemistry · 2009Article
- Co-expression of alpha(1,3)galactosyltransferase and Bacillus thuringiensis PIPLC enhances hyperacute rejection of tumor cells.Cancer immunology, immunotherapy : CII · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Staphylococcus aureus secretes a phosphatidylinositol (PI)-specific phospholipase C (PI-PLC) which is able to hydrolyze the membrane lipid PI and membrane protein anchors containing glycosyl-PI. The gene for PI-PLC (plc) was cloned from S. aureus into Escherichia coli. Oligonucleotide probes based on partial protein sequence and polyclonal antibodies raised against the purified protein were used to identify positive clones. E. coli transformed with a plasmid containing the plc gene expressed PI-PLC enzyme activity which was abolished by mutagenesis with a tetracycline resistance gene. The plc gene was present in all 15 S. aureus strains examined but not in any of 6 coagulase-negative staphylococcal species. The plc gene contained 984 bp and coded for a mature protein with a calculated molecular mass of 34,107 Da. Amino acid sequence comparisons indicated that the staphylococcal plc gene was similar (51 to 56%) to the PI-PLCs from Bacillus cereus, Bacillus thuringiensis, and Listeria monocytogenes. The recombinant PI-PLC expressed in E. coli was purified and exhibited biochemical properties identical to those of the native PI-PLC from S. aureus. PI-PLC production was decreased in agr mutant strains of S. aureus. However, PI-PLC production by both agr+ and agr mutant strains exhibited a similar dependence on the type of medium used. These data suggested that PI-PLC production was regulated by both agr-dependent and agr-independent mechanisms.
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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.