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Interactome of the Legionella pneumophila effector PieE

ABSTRACT: The in vivo interactome of the Legionella pneumophila effector PieE reveals binding to multiple Rab GTPases

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Legionella Pneumophila

DISEASE(S): Legionellosis

SUBMITTER: James Wright

LAB HEAD: Jyoti Choudhary

PROVIDER: PXD000706 | Pride | 2017-02-08

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	OTBEH_Gad1Ctrl.mgf	Mgf
	OTBEH_Gad1Ctrl.raw	Raw
	OTBEH_Gad1Ctrl_MascotPercolator.tab.txt	Txt
	OTBEH_Gad1Ctrl_Pride.pride.mgf.gz	Mgf
	OTBEH_Gad1Ctrl_Pride.pride.mztab.gz	Mztab

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Publications

A new method to determine in vivo interactomes reveals binding of the Legionella pneumophila effector PieE to multiple rab GTPases.

Mousnier Aurélie A Schroeder Gunnar N GN Stoneham Charlotte A CA So Ernest C EC Garnett James A JA Yu Lu L Matthews Steve J SJ Choudhary Jyoti S JS Hartland Elizabeth L EL Frankel Gad G

mBio 20140812 4

<h4>Unlabelled</h4>Legionella pneumophila, the causative agent of Legionnaires' disease, uses the Dot/Icm type IV secretion system (T4SS) to translocate more than 300 effectors into host cells, where they subvert host cell signaling. The function and host cell targets of most effectors remain unknown. PieE is a 69-kDa Dot/Icm effector containing three coiled-coil (CC) regions and 2 transmembrane (TM) helices followed by a fourth CC region. Here, we report that PieE dimerized by an interaction be ...[more]

PMID: 25118235

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Strand specific sequencing illustrates the complex transcriptional response of Legionella pneumophila during infection

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Analysis of secretion of transmembrane effectors by the type IV b secretion system of Legionella pneumophila

Project description:In order to promote intracellular survival and infection, Legionella spp. translocate hundreds of effector proteins into eukaryotic host cells using a type IV b protein secretion system (T4bSS). T4bSS are well known to translocate soluble as well as transmembrane domain-containing effector proteins (TMD-effectors) but the mechanisms of secretion are still poorly understood. Herein we investigated the secretion of hydrophobic TMD-effectors, of which about 80 were previously reported to be encoded by L. pneumophila. A proteomic analysis of fractionated membranes revealed that TMD-effectors are targeted to and inserted into the bacterial inner membranes of L. pneumophila independent of the presence of a functional T4bSS. While the T4bSS chaperones IcmS and IcmW were critical for secretion of all tested TMD-effectors, they did not influence inner membrane targeting of these proteins. The translocation of TMD-effectors into host cells proved to be dependent on a C-terminal secretion signal as it is the case for soluble effector proteins and this signal required presentation towards the cytoplasmic side of the inner membrane. A differential secretion behavior of TMD- and soluble effectors and a need for small periplasmic loops within TMD-effectors provided strong evidence that TMD-effectors are secreted in a two-step secretion process with an inner membrane intermediate that is extracted towards the cytoplasm, possibly by aid of the type IV coupling protein complex, for subsequent secretion into eukaryotic host cells by the T4bSS core complex. Overall, our study highlights the amazing versatility of T4bSS to secrete soluble and TMD-effectors from different subcellular locations of the bacterial cell.

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