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RNAseq profiling of a lpp0148 mutant compared to its isogenic parent Legionella pneumophila strain Paris

ABSTRACT: Comparaison of the transcriptional profile of mutant of the lpp0148 gene and the parent strain Legionella pneumophila strain Paris. lpp0148 codes for a protein with a ProQ domain (PFAM PF04352). A mutant of this gene was obtained by inserting a premature stop codon in the lpp0148 ORF. The lpp0148 mutant is constitutively competent for natural transformation as described here http://www.ncbi.nlm.nih.gov/pubmed/26526572. Transcriptional profiling was done on cultures grown to exponential phase (OD=0.8). Three independent biological replicates were analysed.

INSTRUMENT(S): Illumina HiSeq 2000

ORGANISM(S): Legionella pneumophila

SUBMITTER: Xavier Charpentier

PROVIDER: E-MTAB-4094 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Silencing of natural transformation by an RNA chaperone and a multitarget small RNA.

Attaiech Laetitia L Boughammoura Aïda A Brochier-Armanet Céline C Allatif Omran O Peillard-Fiorente Flora F Edwards Ross A RA Omar Ayat R AR MacMillan Andrew M AM Glover Mark M Charpentier Xavier X

Proceedings of the National Academy of Sciences of the United States of America 20160718 31

A highly conserved DNA uptake system allows many bacteria to actively import and integrate exogenous DNA. This process, called natural transformation, represents a major mechanism of horizontal gene transfer (HGT) involved in the acquisition of virulence and antibiotic resistance determinants. Despite evidence of HGT and the high level of conservation of the genes coding the DNA uptake system, most bacterial species appear non-transformable under laboratory conditions. In naturally transformable ...[more]

PMID: 27432973

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RNAseq profiling of a lpp1663 mutant compared to its isogenic parent Legionella pneumophila strain Paris

Project description:Comparaison of the transcriptional profile of mutant of the lpp1663 gene and the parent strain Legionella pneumophila strain Paris. lpp1663 codes for a protein with a ProQ domain (PFAM PF04352). A mutant of this gene was obtained by deleting the lpp1663 ORF and replacing it with a gene confering resistance to kanamycin. Transcriptional profiling was done on cultures grown to exponential phase (OD=0.8). Three independent biological replicates were analysed.

2020-09-01 | E-MTAB-4095 | biostudies-arrayexpress

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2020-01-27 | PXD001525 | Pride

Transcription profiling by array of Legionella pneumophila ppGpp knockout and relA over expression mutants.

Project description:Effect of ppGpp on transcript level after RelA overexpression (90 min). The cells are constructed in our lab. They are knock-out mutants in the production of ppGpp(guanosine tetraphosphate) of Legionella, complemented with an over-expression vector containing the relA gene to express the RelA protein (responsible for the ppGpp production). The aim is to follow the gene response in Legionella pneumophila after induction of ppGpp at different time points.

2010-04-14 | E-MTAB-211 | biostudies-arrayexpress

Transcription profiling by array of Legionella pneumophilaEfter RelA overexpression.

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2010-04-13 | E-MTAB-222 | biostudies-arrayexpress

Transcription profiling of Dictyostelium discoideum wild type and dupA null after infection with Legionella pneumophila

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

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2010-11-25 | E-MTAB-164 | biostudies-arrayexpress

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2013-05-21 | E-GEOD-42905 | biostudies-arrayexpress

Migration of Acanthamoeba through Legionella biofilms is regulated by bacterial quorum sensing, effectors and the flagellum

Project description:Legionella pneumophila is a Gram-negative, environmental bacterium, which causes the life-threatening pneumonia Legionnaires’ disease. The facultative intracellular bacterium forms biofilms and employs the Icm/Dot type IV secretion system (T4SS) to replicate in amoebae and macrophages. The Legionella quorum sensing (Lqs) system and the transcription factor LvbR form a regulatory network controlling various traits, including bacterial motility, virulence and biofilm architecture. Here we show by comparative proteomics that in biofilms formed by L. pneumophila mutant strains lacking LvbR or the response regulator LqsR, proteins encoded by the 133 kb fitness island and components of the flagellum (FlaA) are downregulated. Confocal microscopy revealed that the ∆lqsR or ∆flaA mutant strains formed biofilms of the same patchy morphology as the parental strain JR32, while the ∆lvbR mutant forms a mat-like biofilm as previously shown. Acanthamoeba castellanii amoebae migrated more slowly through biofilms formed by the ∆lvbR, ∆lqsR or ∆flaA mutant strains, and amoebae migration was impaired in biofilms formed by L. pneumophila lacking a functional Icm/Dot T4SS (∆icmT) or the secreted effector proteins LegG1 and PpgA. Amoebae migrating through biofilms formed by JR32, ∆lvbR or ∆icmT were decorated by clusters of bacteria, while amoebae in ∆lqsR or ∆flaA biofilms were not. Taken together, the Lqs system, LvbR, FlaA and the Icm/Dot T4SS regulate migration of A. castellanii through L. pneumophila biofilms, and – with the exception of the T4SS – also regulate bacterial cluster formation on the amoeba. Hence, amoebae migration through L. pneumophila biofilms is regulated by bacterial quorum sensing, virulence and motility.

2022-06-08 | PXD030337 | Pride

The Legionella-driven PtdIns(4)P gradient at LCV-ER membrane contact sites promotes Vap-, OSBP and Sac1-dependent pathogen vacuole remodeling

Project description:The causative agent of Legionnaires’ disease, Legionella pneumophila, governs interactions with host cells by secreting ca. 330 different “effector” proteins. The facultative intracellular bacteria replicate in macrophages and amoeba within a unique compartment, the Legionella-containing vacuole (LCV). Hallmarks of LCV formation are the phosphoinositide (PI) lipid conversion from PtdIns(3)P to PtdIns(4)P, fusion with endoplasmic reticulum (ER)-derived vesicles and a tight association with the ER. Proteomics of purified LCVs revealed the presence of membrane contact sites (MCS) proteins implicated in lipid exchange. Using dually fluorescence-labeled Dictyostelium discoideum amoeba, we reveal that the VAMP-associated protein (Vap), the PtdIns(4)P 4-phosphatase Sac1, and the large fusion GTPase Sey1/atlastin-3 localize to the ER, but not to the LCV membrane, and these ER-resident proteins promote intracellular replication of L. pneumophila and LCV remodeling. Moreover, oxysterol binding proteins (OSBPs) exclusively localize to the ER (OsbH) or the LCV membrane (OsbK), respectively, and promote (OsbH) or restrict (OsbK) intracellular replication of L. pneumophila and LCV expansion. Furthermore, the PtdIns(4)P-subverting L. pneumophila effectors LepB and SidC also promote LCV remodeling. Taken together, the Legionella-driven PtdIns(4)P gradient at LCV-ER MCSs promotes Vap-, OSBP- and Sac1-dependent pathogen vacuole remodeling.

2023-02-21 | PXD034490 | Pride

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