ArticleThe Journal of biological chemistry2014
A type IV translocated Legionella cysteine phytase counteracts intracellular growth restriction by phytate.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Identifying Opportunity Targets in Gram-Negative Pathogens for Infectious Disease Mitigation.ACS central science · 2025Review
- Article
- Insights into the role of legionella effectors on host metabolic perturbations.Frontiers in cellular and infection microbiology · 2024Review
- Concept about the Virulence Factor ofMicroorganisms · 2022Review
- An Extracytoplasmic Function Sigma Factor Required for Full Virulence in Xanthomonas citri pv. citri.Journal of bacteriology · 2022Article
- Phosphoinositides and the Fate ofFrontiers in immunology · 2020Review
- Characteristics of the First Protein Tyrosine Phosphatase with Phytase Activity from a Soil Metagenome.Genes · 2019Article
- Article
- Review
- A 1-phytase type III effector interferes with plant hormone signaling.Nature communications · 2017Article
- Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.Nature communications · 2017Article
- Bacterial PhyA protein-tyrosine phosphatase-likeThe Journal of biological chemistry · 2017Article
- Intra-Species and Inter-Kingdom Signaling ofFrontiers in microbiology · 2017Review
- Metabolism of myo-Inositol by Legionella pneumophila Promotes Infection of Amoebae and Macrophages.Applied and environmental microbiology · 2016Article
- Subversion of Cell-Autonomous Immunity and Cell Migration by Legionella pneumophila Effectors.Frontiers in immunology · 2015Review
- An investigation of virulence factors of Legionella pneumophila environmental isolates.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The causative agent of Legionnaires' pneumonia, Legionella pneumophila, colonizes diverse environmental niches, including biofilms, plant material, and protozoa. In these habitats, myo-inositol hexakisphosphate (phytate) is prevalent and used as a phosphate storage compound or as a siderophore. L. pneumophila replicates in protozoa and mammalian phagocytes within a unique "Legionella-containing vacuole." The bacteria govern host cell interactions through the Icm/Dot type IV secretion system (T4SS) and ∼300 different "effector" proteins. Here we characterize a hitherto unrecognized Icm/Dot substrate, LppA, as a phytate phosphatase (phytase). Phytase activity of recombinant LppA required catalytically essential cysteine (Cys(231)) and arginine (Arg(237)) residues. The structure of LppA at 1.4 Å resolution revealed a mainly α-helical globular protein stabilized by four antiparallel β-sheets that binds two phosphate moieties. The phosphates localize to a P-loop active site characteristic of dual specificity phosphatases or to a non-catalytic site, respectively. Phytate reversibly abolished growth of L. pneumophila in broth, and growth inhibition was relieved by overproduction of LppA or by metal ion titration. L. pneumophila lacking lppA replicated less efficiently in phytate-loaded Acanthamoeba castellanii or Dictyostelium discoideum, and the intracellular growth defect was complemented by the phytase gene. These findings identify the chelator phytate as an intracellular bacteriostatic component of cell-autonomous host immunity and reveal a T4SS-translocated L. pneumophila phytase that counteracts intracellular bacterial growth restriction by phytate. Thus, bacterial phytases might represent therapeutic targets to combat intracellular pathogens.
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