PXD034490 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The Legionella-driven PtdIns(4)P gradient at LCV-ER membrane contact sites promotes Vap-, OSBP and Sac1-dependent pathogen vacuole remodeling |
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. |
HostingRepository | PRIDE |
AnnounceDate | 2023-02-21 |
AnnouncementXML | Submission_2023-02-21_09:08:11.874.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | SandraMaass |
SpeciesList | scientific name: Legionella pneumophila subsp. pneumophila str. Philadelphia 1; NCBI TaxID: NCBITaxon:272624; scientific name: Dictyostelium discoideum; NCBI TaxID: NCBITaxon:44689; |
ModificationList | acetylated residue; monohydroxylated residue |
Instrument | LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-06-13 02:08:02 | ID requested | |
⏵ 1 | 2023-02-21 09:08:12 | announced | |
2 | 2023-11-14 07:28:35 | announced | 2023-11-14: Updated project metadata. |
Publication List
Vormittag S, H, ü, sler D, Haneburger I, Kroniger T, Anand A, Prantl M, Barisch C, Maa, ß S, Becher D, Letourneur F, Hilbi H, Legionella- and host-driven lipid flux at LCV-ER membrane contact sites promotes vacuole remodeling. EMBO Rep, 24(3):e56007(2023) [pubmed] |
Keyword List
submitter keyword: large fusion GTPase, oxysterol binding protein, Legionella pneumophila, atlastin, Legionnaires’ disease, host-pathogen interaction, pathogen vacuole,Amoeba, Dictyostelium discoideum |
Contact List
DörteBecher |
contact affiliation | Institute of Microbiology, University of Greifswald, Felix-Hausdorff-Strasse 8, 17489 Greifswald, Germany |
contact email | dbecher@uni-greifswald.de |
lab head | |
SandraMaass |
contact affiliation | University of Greifswald, Department for Microbial Proteomics |
contact email | sandra.maass@uni-greifswald.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD034490
- Label: PRIDE project
- Name: The Legionella-driven PtdIns(4)P gradient at LCV-ER membrane contact sites promotes Vap-, OSBP and Sac1-dependent pathogen vacuole remodeling