PXD020161

PXD020161 is an original dataset announced via ProteomeXchange.

Title	Shigella hijacks the exocyst to cluster macropinosomes for efficient vacuolar escape
Description	Shigella flexneri invades host cells by entering within a bacteria-containing vacuole (BCV). In order to establish its niche in the host cytosol, the bacterium ruptures its BCV. Contacts between S. flexneri BCV and infection-associated macropinosomes (IAMs) formed in situ have been reported to enhance BCV disintegration. The mechanism underlying S. flexneri vacuolar escape remains however obscure. To decipher the molecular mechanism priming the communication between the IAMs and S. flexneri BCV, we performed mass spectrometry-based analysis of the magnetically purified IAMs from S. flexneri-infected cells. While proteins involved in host recycling and exocytic pathways were significantly enriched at the IAMs, we demonstrate more precisely that the S. flexneri type III effector protein IpgD mediates the recruitment of the exocyst to the IAMs through the Rab8/Rab11 pathway. This recruitment results in IAM clustering around S. flexneri BCV. More importantly, we reveal that IAM clustering subsequently facilitates an IAM-mediated unwrapping of the ruptured vacuole membranes from S. flexneri, enabling the naked bacterium to be ready for intercellular spread via actin-based motility. Taken together, our work untangles the molecular cascade of S. flexneri-driven host trafficking subversion at IAMs to develop its cytosolic lifestyle, a crucial step en route for infection progression at cellular and tissue level.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:24:34.564.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Magalie Duchateau
SpeciesList	scientific name: Shigella flexneri 5a str. M90T; NCBI TaxID: 1086030;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2020-07-02 17:05:49	ID requested
1	2021-08-11 01:31:40	announced
⏵ 2	2024-10-22 05:24:39	announced	2024-10-22: Updated project metadata.

Chang YY, St, é, venin V, Duchateau M, Giai Gianetto Q, Hourdel V, Rodrigues CD, Matondo M, Reiling N, Enninga J, Shigella hijacks the exocyst to cluster macropinosomes for efficient vacuolar escape. PLoS Pathog, 16(8):e1008822(2020) [pubmed]

10.1371/journal.ppat.1008822;

submitter keyword: macropinosomes,Shigella

Jost Enninga
contact affiliation	Institut Pasteur Unité de Dynamique des interactions hôte-pathogène 25, rue du Docteur Roux 75015 Paris, France
contact email	jost.enninga@pasteur.fr
lab head
Magalie Duchateau
contact affiliation	Institut Pasteur
contact email	magalie.duchateau@pasteur.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/08/PXD020161

PRIDE project URI

• PRIDE
  1. PXD020161
     1. Label: PRIDE project
     2. Name: Shigella hijacks the exocyst to cluster macropinosomes for efficient vacuolar escape