ArticleInfection and immunity2013
LtpD is a novel Legionella pneumophila effector that binds phosphatidylinositol 3-phosphate and inositol monophosphatase IMPA1.
Article in Infection and immunity, 2013. 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.
- Concept about the Virulence Factor ofMicroorganisms · 2022Review
- Knowledge to Predict Pathogens:Microorganisms · 2022Review
- A Small Protein but with Diverse Roles: A Review of EsxA in Mycobacterium-Host Interaction.Cells · 2021Review
- Phosphoinositides and the Fate ofFrontiers in immunology · 2020Review
- SopF, a phosphoinositide binding effector, promotes the stability of the nascent Salmonella-containing vacuole.PLoS pathogens · 2019Article
- Study ofInfection and immunity · 2019Article
- TheThe Journal of biological chemistry · 2019Article
- PIKfyve/Fab1 is required for efficient V-ATPase and hydrolase delivery to phagosomes, phagosomal killing, and restriction of Legionella infection.PLoS pathogens · 2019Article
- A Phosphatidylinositol 3-Kinase Effector Alters Phagosomal Maturation to Promote Intracellular Growth of Francisella.Cell host & microbe · 2018Article
- Salmonella Typhi Colonization Provokes Extensive Transcriptional Changes Aimed at Evading Host Mucosal Immune Defense During Early Infection of Human Intestinal Tissue.EBioMedicine · 2018Article
- Differences in Virulence BetweenFrontiers in cellular and infection microbiology · 2018Article
- The Toolbox for Uncovering the Functions ofFrontiers in cellular and infection microbiology · 2017Review
- Legionella pneumophila Effector LpdA Is a Palmitoylated Phospholipase D Virulence Factor.Infection and immunity · 2015Article
- Targeting of the hydrophobic metabolome by pathogens.Traffic (Copenhagen, Denmark) · 2015Review
- Subversion of Cell-Autonomous Immunity and Cell Migration by Legionella pneumophila Effectors.Frontiers in immunology · 2015Review
- Article
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Authors and funding
7 authors.
Funding
Abstract
The Dot/Icm type IV secretion system (T4SS) of Legionella pneumophila is crucial for the pathogen to survive in protozoa and cause human disease. Although more than 275 effector proteins are delivered into the host cell by the T4SS, the function of the majority is unknown. Here we have characterized the Dot/Icm effector LtpD. During infection, LtpD localized to the cytoplasmic face of the membrane of the Legionella-containing vacuole (LCV). In A549 lung epithelial cells, ectopically expressed LtpD localized to large vesicular structures that contained markers of endosomal compartments. Systematic analysis of LtpD fragments identified an internal 17-kDa fragment, LtpD471-626, which was essential for targeting ectopically expressed LtpD to vesicular structures and for the association of translocated LtpD with the LCV. LtpD471-626 bound directly to phosphatidylinositol 3-phosphate [PtdIns(3)P] in vitro and colocalized with the PtdIns(3)P markers FYVE and SetA in cotransfected cells. LtpD was also found to bind the host cell enzyme inositol (myo)-1 (or 4)-monophosphatase 1, an important phosphatase involved in phosphoinositide production. Analysis of the role of LtpD in infection showed that LtpD is involved in bacterial replication in THP-1 macrophages, the larvae of Galleria mellonella, and mouse lungs. Together, these data suggest that LtpD is a novel phosphoinositide-binding L. pneumophila effector that has a role in intracellular bacterial replication.
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