PXD037166 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Cells responding to bacterial pore-forming toxins release extracellular vesicles displaying similar proteomic content |
Description | The plasma membrane (PM) protects cells from extracellular threats and supports cellular homeostasis. Some pathogens produce pore-forming toxins (PFTs) that disrupt PM integrity by forming transmembrane pores. High PFT concentrations cause massive damage leading to cell death and facilitating infection. Sub-lytic PFT doses activate repair mechanisms to restore PM integrity, support cell survival and limit disease. Shedding of extracellular vesicles (EVs) was proposed as a mechanism to eliminate PFTs pores and restore PM integrity. We show here that indeed PFTs are at least partially eliminated through EV release and hypothesized that proteins important for PM repair might be included in EVs shed by cells during repair. To identify new PM repair proteins, we collected EVs released by cells challenged with sub-lytic doses of two different PFTs, Listeriolysin O and Pneumolysin, and determined their proteomic repertoire by LC-MS/MS analysis. Intoxicated cells release similar EVs irrespectively of the PFT used. Also, they release more and larger EVs than non-intoxicated cells. A cluster of 76 proteins including calcium-binding proteins, molecular chaperones, cytoskeletal, scaffold and membrane trafficking proteins, was detected enriched in EVs collected from intoxicated cells. While some of these proteins have well-characterized roles in repair, the involvement of others requires further studies. We reveal here new proteins potentially involved in PM repair and give new insights into common mechanisms and machinery engaged by cells in response to PM damage. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_07:34:34.296.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Rupert Mayer |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-10-03 11:40:36 | ID requested | |
1 | 2023-02-10 06:04:38 | announced | |
⏵ 2 | 2023-11-14 07:34:35 | announced | 2023-11-14: Updated project metadata. |
Publication List
Alves S, Pereira JM, Mayer RL, Gon, ç, alves ADA, Impens F, Cabanes D, Sousa S, Cells Responding to Closely Related Cholesterol-Dependent Cytolysins Release Extracellular Vesicles with a Common Proteomic Content Including Membrane Repair Proteins. Toxins (Basel), 15(1):(2022) [pubmed] |
Keyword List
submitter keyword: calcium influx, shedding, extracellular vesicles, HeLa, listeriolysin O, label-free, pneumolysin,Q Exactive, pore-forming toxins, plasma membrane repair |
Contact List
Sandra Sousa |
contact affiliation | Cell Biology of Bacterial Infections, IBMC, i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Portugal |
contact email | srsousa@ibmc.up.pt |
lab head | |
Rupert Mayer |
contact affiliation | VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium. |
contact email | rupert.mayer@vib-ugent.be |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD037166
- Label: PRIDE project
- Name: Cells responding to bacterial pore-forming toxins release extracellular vesicles displaying similar proteomic content