ArticleInfection and immunity2004
Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 67 citations in OpenAlex.
- Comparative analysis of Legionella lytica genome identifies specific metabolic traits and virulence factors.Scientific reports · 2025Article
- NAD(H)-mediated tetramerization controls the activity ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Virulence Traits of Environmental and Clinical Legionella pneumophila Multilocus Variable-Number Tandem-Repeat Analysis (MLVA) Genotypes.Applied and environmental microbiology · 2018Article
- Disulfide loop cleavage of Legionella pneumophila PlaA boosts lysophospholipase A activity.Scientific reports · 2017Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Molecular & cellular proteomics : MCP · 2016Article
- Oligomerization inhibits Legionella pneumophila PlaB phospholipase A activity.The Journal of biological chemistry · 2014Article
- Nutrient salvaging and metabolism by the intracellular pathogen Legionella pneumophila.Frontiers in cellular and infection microbiology · 2014Review
- Characterization of Plp, a phosphatidylcholine-specific phospholipase and hemolysin of Vibrio anguillarum.BMC microbiology · 2013Article
- Chromobacterium violaceum: important insights for virulence and biotechnological potential by exoproteomic studies.Current microbiology · 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
- Regulation, integrase-dependent excision, and horizontal transfer of genomic islands in Legionella pneumophila.Journal of bacteriology · 2013Article
- Zinc metalloproteinase ProA directly activates Legionella pneumophila PlaC glycerophospholipid:cholesterol acyltransferase.The Journal of biological chemistry · 2012Article
- Isotopologue profiling of Legionella pneumophila: role of serine and glucose as carbon substrates.The Journal of biological chemistry · 2010Article
- Molecular pathogenesis of infections caused by Legionella pneumophila.Clinical microbiology reviews · 2010Review
- Lipids in host-pathogen interactions: pathogens exploit the complexity of the host cell lipidome.Progress in lipid research · 2010Review
- Phospholipase PlaB of Legionella pneumophila represents a novel lipase family: protein residues essential for lipolytic activity, substrate specificity, and hemolysis.The Journal of biological chemistry · 2009Article
- bdhA-patD operon as a virulence determinant, revealed by a novel large-scale approach for identification of Legionella pneumophila mutants defective for amoeba infection.Applied and environmental microbiology · 2009Article
- Identification and characterization of hemolysin-like proteins similar to RTX toxin in Pasteurella pneumotropica.Journal of bacteriology · 2009Article
- Multiple roles of phospholipase A2 during lung infection and inflammation.Infection and immunity · 2008Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Legionella pneumophila, the causative agent of Legionnaires' disease, is an intracellular pathogen of amoebae, macrophages, and epithelial cells. The pathology of Legionella infections involves alveolar cell destruction, and several proteins of L. pneumophila are known to contribute to this ability. By screening a genomic library of L. pneumophila, we found an additional L. pneumophila gene, plaB, which coded for a hemolytic activity and contained a lipase consensus motif in its deduced protein sequence. Moreover, Escherichia coli harboring the L. pneumophila plaB gene showed increased activity in releasing fatty acids predominantly from diacylphospho- and lysophospholipids, demonstrating that it encodes a phospholipase A. It has been reported that culture supernatants and cell lysates of L. pneumophila possess phospholipase A activity; however, only the major secreted lysophospholipase A PlaA has been investigated on the molecular level. We therefore generated isogenic L. pneumophila plaB mutants and tested those for hemolysis, lipolytic activities, and intracellular survival in amoebae and macrophages. Compared to wild-type L. pneumophila, the plaB mutant showed reduced hemolysis of human red blood cells and almost completely lost its cell-associated lipolytic activity. We conclude that L. pneumophila plaB is the gene encoding the major cell-associated phospholipase A, possibly contributing to bacterial cytotoxicity due to its hemolytic activity. On the other hand, in view of the fact that the plaB mutant multiplied like the wild type both in U937 macrophages and in Acanthamoeba castellanii amoebae, plaB is not essential for intracellular survival of the pathogen.
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