ArticleInfection and immunity2005
Characterization of the major secreted zinc metalloprotease- dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila.
Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 76 citations in OpenAlex.
- Mucin stimulates the growth ofMicrobiology (Reading, England) · 2026Article
- Cellular cholesterol licensesMicrobial cell (Graz, Austria) · 2023Article
- Protein sociology of ProA, Mip and other secreted virulence factors at theFrontiers in cellular and infection microbiology · 2023Review
- Concept about the Virulence Factor ofMicroorganisms · 2022Review
- Review
- Vibrio deploys type 2 secreted lipase to esterify cholesterol with host fatty acids and mediate cell egress.eLife · 2020Article
- Assessing the impact, genomics and evolution of type II secretion across a large, medically important genus: the Legionella type II secretion paradigm.Microbial genomics · 2019Article
- Novel type of pilus associated with a Shiga-toxigenic E. coli hybrid pathovar conveys aggregative adherence and bacterial virulence.Emerging microbes & infections · 2018Article
- Article
- Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity.Scientific reports · 2017Article
- Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Molecular & cellular proteomics : MCP · 2016Article
- The novel Legionella pneumophila type II secretion substrate NttC contributes to infection of amoebae Hartmannella vermiformis and Willaertia magna.Microbiology (Reading, England) · 2014Article
- Oligomerization inhibits Legionella pneumophila PlaB phospholipase A activity.The Journal of biological chemistry · 2014Article
- Multiple Legionella pneumophila Type II secretion substrates, including a novel protein, contribute to differential infection of the amoebae Acanthamoeba castellanii, Hartmannella vermiformis, and Naegleria lovaniensis.Infection and immunity · 2013Article
- The Legionella pneumophila Dot/Icm-secreted effector PlcC/CegC1 together with PlcA and PlcB promotes virulence and belongs to a novel zinc metallophospholipase C family present in bacteria and fungi.The Journal of biological chemistry · 2013Article
- Zinc metalloproteinase ProA directly activates Legionella pneumophila PlaC glycerophospholipid:cholesterol acyltransferase.The Journal of biological chemistry · 2012Article
- Legionella pneumophila type II secretion dampens the cytokine response of infected macrophages and epithelia.Infection and immunity · 2011Article
- Molecular pathogenesis of infections caused by Legionella pneumophila.Clinical microbiology reviews · 2010Review
- Temporal and spatial trigger of post-exponential virulence-associated regulatory cascades by Legionella pneumophila after bacterial escape into the host cell cytosol.Environmental microbiology · 2010Article
- Lipids in host-pathogen interactions: pathogens exploit the complexity of the host cell lipidome.Progress in lipid research · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legionella pneumophila, an intracellular pathogen causing a severe pneumonia, possesses distinct lipolytic activities which have not been completely assigned to specific enzymes so far. We cloned and characterized a gene, plaC, encoding a protein with high homology to PlaA, the major secreted lysophospholipase A of L. pneumophila and to other hydrolytic enzymes belonging to the GDSL family. Here we show that L. pneumophila plaC mutants possessed reduced phospholipase A and lysophospholipase A activities and lacked glycerophospholipid:cholesterol acyltransferase activity in their culture supernatants. The mutants' reduced phospholipase A and acyltransferase activities were complemented by reintroduction of an intact copy of plaC. Additionally, plaC conferred increased lysophospholipase A and glycerophospholipid:cholesterol acytransferase activities to recombinant Escherichia coli. Furthermore, PlaC was shown to be another candidate exported by the L. pneumophila type II secretion system and was activated by a factor present in the bacterial culture supernatant dependent on the zinc metalloprotease. Finally, the role of plaC in intracellular infection of Acanthamoeba castellanii and U937 macrophages with L. pneumophila was assessed, and plaC was found to be dispensable. Thus, L. pneumophila possesses another secreted lipolytic enzyme, a protein with acyltransferase, phospholipase A, and lysophospholipase A activities. This enzyme is distinguished from the previously characterized phospholipases A and lysophospholipases A by its capacity not only to cleave fatty acids from lipids but to transfer them to cholesterol. Cholesterol is an important compound of eukaryotic membranes, and an acyltransferase might be a tool for host cell modification to fit the needs of the bacterium.
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