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Legionella pneumophila proteome

ABSTRACT: Legionella pneumophila cells were harvested during exponential growth (RP) and stationary growth (TP). VBNC cells were also anylzed. Protein subfractions were studied.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Legionella Pneumophila Subsp. Pneumophila (strain Philadelphia 1 / Atcc 33152 / Dsm 7513)

TISSUE(S): Cell

SUBMITTER: Birgit Voigt

LAB HEAD: Miacheal Hecker

PROVIDER: PXD001926 | Pride | 2015-11-13

REPOSITORIES: Pride

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			Action	DRS
	120330_O2_P1_SG_BV_RPR1_1.RAW	Raw
	120330_O2_P1_SG_BV_RPR1_10.RAW	Raw
	120330_O2_P1_SG_BV_RPR1_2.RAW	Raw
	120330_O2_P1_SG_BV_RPR1_3.RAW	Raw
	120330_O2_P1_SG_BV_RPR1_4.RAW	Raw

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Publications

Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.

Aurass Philipp P Gerlach Thomas T Becher Dörte D Voigt Birgit B Karste Susanne S Bernhardt Jörg J Riedel Katharina K Hecker Michael M Flieger Antje A

Molecular & cellular proteomics : MCP 20151106 1

Major differences in the transcriptional program underlying the phenotypic switch between exponential and post-exponential growth of Legionella pneumophila were formerly described characterizing important alterations in infection capacity. Additionally, a third state is known where the bacteria transform in a viable but nonculturable state under stress, such as starvation. We here describe phase-related proteomic changes in exponential phase (E), postexponential phase (PE) bacteria, and uncultur ...[more]

PMID: 26545400

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

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Project description:The intracellular bacterial pathogen Legionella pneumophila (L.p.) manipulates eukaryotic host ubiquitination machinery to form its replicative vacuole. While nearly 10% of L.p.’s ∼330 secreted effector proteins are ubiquitin ligases or deubiquitinases, a comprehensive measure of temporally resolved changes in the endogenous host ubiquitinome during infection has not been undertaken. To elucidate how L.p hijacks host cell ubiquitin signaling, we generated a proteome-wide analysis of changes in protein ubiquitination during infection. We discover that L.p. infection increases ubiquitination of host regulators of subcellular trafficking and membrane dynamics, most notably ∼40% of mammalian Ras superfamily small GTPases. We determine that these small GTPases undergo non-degradative ubiquitination at the Legionella-containing vacuole membrane. Finally, we find that the bacterial effectors SidC/SdcA play a central role in cross-family small GTPase ubiquitination, and that these effectors function upstream of SidE-family ligases in the poly-ubiquitination and retention of GTPases in the LCV membrane. This work highlights the extensive reconfiguration of host ubiquitin signaling by bacterial effectors during infection and establishes simultaneous ubiquitination of small GTPases across the Ras superfamily as a novel consequence of L.p. infection. Our findings position L.p. as a tool to better understand how small GTPases can be regulated by ubiquitination in uninfected contexts.

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Comparative proteomics of purified pathogen vacuoles correlates intracellular replication of Legionella pneumophila with the small GTPase Rap1

Project description:Legionella pneumophila is an opportunistic bacterial pathogen that causes a severe lung infection termed “Legionnaires’ disease”. The pathogen replicates in environmental protozoa as well as in macrophages within a unique membrane-bound compartment, the Legionella-containing-vacuole (LCV). Formation of the pathogen vacuole requires the bacterial Icm/Dot type IV secretion system (T4SS), which translocates ca. 300 effector proteins into host cells, where they subvert pivotal host processes and govern LCV formation. The L. pneumophila “pentuple” mutant lacks 5 gene clusters comprising 12% of the genome and 30% of the effector proteins. The mutant strain replicates in murine bone marrow-derived macrophages but not in Dictyostelium discoideum amoeba. In order to elucidate the host cell proteome defining a replication permissive compartment, we compare here the proteomes of intact LCVs isolated from D. discoideum or murine RAW 264.7 macrophages infected with the L. pneumophila parental strain Lp02 or the “pentuple” mutant. Proteome analysis by liquid chromatography-tandem mass spectrometry (LC-MS/MS) revealed host proteins specifically localizing to LCVs harbouring strain Lp02 or the “pentuple” mutant, respectively. The small GTPase Rap1 was identified on D. discoideum LCVs containing strain Lp02 but not the “pentuple” mutant and on macrophage LCVs containing either strain. The localization pattern of Rap1 on D. discoideum LCVs was confirmed by fluorescence microscopy, and depletion of Rap1 in A549 epithelial cells by RNA interference significantly reduced the intracellular growth of L. pneumophila. Thus, comparative proteomics identified Rap1 as a novel LCV host component implicated in intracellular replication of L. pneumophila.

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