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dc.contributor.author
Weber, Stefan S.
dc.contributor.author
Ragaz, Curdin
dc.contributor.author
Reus, Katrin
dc.contributor.author
Nyfeler, Yves
dc.contributor.author
Hilbi, Hubert
dc.date.accessioned
2018-11-27T11:49:44Z
dc.date.available
2017-06-08T15:13:50Z
dc.date.available
2018-11-05T11:04:17Z
dc.date.available
2018-11-06T09:41:07Z
dc.date.available
2018-11-27T11:49:44Z
dc.date.issued
2006-05-19
dc.identifier.issn
1553-7374
dc.identifier.issn
1553-7366
dc.identifier.other
10.1371/journal.ppat.0020046
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/702
dc.identifier.doi
10.3929/ethz-b-000000702
dc.description.abstract
The causative agent of Legionnaires' disease, Legionella pneumophila, employs the intracellular multiplication (Icm)/defective organelle trafficking (Dot) type IV secretion system (T4SS) to upregulate phagocytosis and to establish a replicative vacuole in amoebae and macrophages. Legionella-containing vacuoles (LCVs) do not fuse with endosomes but recruit early secretory vesicles. Here we analyze the role of host cell phosphoinositide (PI) metabolism during uptake and intracellular replication of L. pneumophila. Genetic and pharmacological evidence suggests that class I phosphatidylinositol(3) kinases (PI3Ks) are dispensable for phagocytosis of wild-type L. pneumophila but inhibit intracellular replication of the bacteria and participate in the modulation of the LCV. Uptake and degradation of an icmT mutant strain lacking a functional Icm/Dot transporter was promoted by PI3Ks. We identified Icm/Dot–secreted proteins which specifically bind to phosphatidylinositol(4) phosphate (PI(4)P) in vitro and preferentially localize to LCVs in the absence of functional PI3Ks. PI(4)P was found to be present on LCVs using as a probe either an antibody against PI(4)P or the PH domain of the PI(4)P-binding protein FAPP1 (phosphatidylinositol(4) phosphate adaptor protein-1). Moreover, the presence of PI(4)P on LCVs required a functional Icm/Dot T4SS. Our results indicate that L. pneumophila modulates host cell PI metabolism and exploits the Golgi lipid second messenger PI(4)P to anchor secreted effector proteins to the LCV.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
PLOS
dc.rights.uri
http://creativecommons.org/licenses/by/2.0/
dc.title
Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 2.0 Generic
ethz.journal.title
PLoS Pathogens
ethz.journal.volume
2
en_US
ethz.journal.issue
5
en_US
ethz.journal.abbreviated
PLoS Pathog
ethz.pages.start
e46
en_US
ethz.size
13 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.publication.place
Lawrence, KS
ethz.publication.status
published
en_US
ethz.leitzahl
03618 - Hilbi, Hubert (SNF-Professur)
en_US
ethz.leitzahl.certified
03618 - Hilbi, Hubert (SNF-Professur)
ethz.date.deposited
2017-06-08T15:14:12Z
ethz.source
ECIT
ethz.identifier.importid
imp59364b303715654698
ethz.ecitpid
pub:10462
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-26T19:59:00Z
ethz.rosetta.lastUpdated
2024-02-02T06:41:31Z
ethz.rosetta.versionExported
true
ethz.COinS
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