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Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella

The facultative intracellular pathogen Legionella pneumophila replicates in free-living amoebae and macrophages within a distinct compartment, the “Legionella-containing vacuole” (LCV). LCV formation involves phosphoinositide (PI) glycerolipids, which are key factors controlling vesicle trafficking...

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Autores principales: Hilbi, Hubert, Weber, Stephen, Finsel, Ivo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153050/
https://www.ncbi.nlm.nih.gov/pubmed/21833330
http://dx.doi.org/10.3389/fmicb.2011.00091
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author Hilbi, Hubert
Weber, Stephen
Finsel, Ivo
author_facet Hilbi, Hubert
Weber, Stephen
Finsel, Ivo
author_sort Hilbi, Hubert
collection PubMed
description The facultative intracellular pathogen Legionella pneumophila replicates in free-living amoebae and macrophages within a distinct compartment, the “Legionella-containing vacuole” (LCV). LCV formation involves phosphoinositide (PI) glycerolipids, which are key factors controlling vesicle trafficking pathways and membrane dynamics of eukaryotic cells. To govern the interactions with host cells, L. pneumophila employs the Icm/Dot type IV secretion system and more than 250 translocated “effector proteins” that presumably subvert host signaling and vesicle trafficking pathways. Some of the effector proteins anchor through distinct PIs to the cytosolic face of LCVs and promote the interaction with host vesicles and organelles, catalyze guanine nucleotide exchange of small GTPases, or bind to PI-metabolizing enzymes, such as OCRL1. The PI 5-phosphatase OCRL1 and its Dictyostelium homologue Dd5P4 restrict intracellular growth of L. pneumophila. Moreover, OCRL1/Dd5P4, PI 3-kinases (PI3Ks), and PI4KIIIβ regulate LCV formation and localization of the effector protein SidC, which selectively decorates the LCV membrane. SidC and its 20-kDa “P4C” fragment are robust and specific probes for phosphatidylinositol-4-phosphate, and SidC can be targeted to purify intact LCVs by immuno-magnetic separation. Taken together, bacterial PI-binding effectors as well as host PIs and PI-modulating enzymes play a pivotal role for intracellular replication of L. pneumophila, and the PI-binding effectors are valuable tools for the analysis of eukaryotic PI lipids.
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spelling pubmed-31530502011-08-10 Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella Hilbi, Hubert Weber, Stephen Finsel, Ivo Front Microbiol Microbiology The facultative intracellular pathogen Legionella pneumophila replicates in free-living amoebae and macrophages within a distinct compartment, the “Legionella-containing vacuole” (LCV). LCV formation involves phosphoinositide (PI) glycerolipids, which are key factors controlling vesicle trafficking pathways and membrane dynamics of eukaryotic cells. To govern the interactions with host cells, L. pneumophila employs the Icm/Dot type IV secretion system and more than 250 translocated “effector proteins” that presumably subvert host signaling and vesicle trafficking pathways. Some of the effector proteins anchor through distinct PIs to the cytosolic face of LCVs and promote the interaction with host vesicles and organelles, catalyze guanine nucleotide exchange of small GTPases, or bind to PI-metabolizing enzymes, such as OCRL1. The PI 5-phosphatase OCRL1 and its Dictyostelium homologue Dd5P4 restrict intracellular growth of L. pneumophila. Moreover, OCRL1/Dd5P4, PI 3-kinases (PI3Ks), and PI4KIIIβ regulate LCV formation and localization of the effector protein SidC, which selectively decorates the LCV membrane. SidC and its 20-kDa “P4C” fragment are robust and specific probes for phosphatidylinositol-4-phosphate, and SidC can be targeted to purify intact LCVs by immuno-magnetic separation. Taken together, bacterial PI-binding effectors as well as host PIs and PI-modulating enzymes play a pivotal role for intracellular replication of L. pneumophila, and the PI-binding effectors are valuable tools for the analysis of eukaryotic PI lipids. Frontiers Research Foundation 2011-04-27 /pmc/articles/PMC3153050/ /pubmed/21833330 http://dx.doi.org/10.3389/fmicb.2011.00091 Text en Copyright © 2011 Hilbi, Weber and Finsel. http://www.frontiersin.org/licenseagreement This is an open-access article subject to a non-exclusive license between the authors and Frontiers Media SA, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and other Frontiers conditions are complied with.
spellingShingle Microbiology
Hilbi, Hubert
Weber, Stephen
Finsel, Ivo
Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title_full Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title_fullStr Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title_full_unstemmed Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title_short Anchors for Effectors: Subversion of Phosphoinositide Lipids by Legionella
title_sort anchors for effectors: subversion of phosphoinositide lipids by legionella
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153050/
https://www.ncbi.nlm.nih.gov/pubmed/21833330
http://dx.doi.org/10.3389/fmicb.2011.00091
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