PXD006212-2

PXD006212 is an original dataset announced via ProteomeXchange.

Title	Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4
Description	Neisseria meningitidis (meningococcus) is an invasive bacterial pathogen that colonizes human vessels, causing thrombotic lesions and meningitis. Establishment of tight interactions with endothelial cells is crucial for meningococci to resist hemodynamic forces. Two endothelial receptors, CD147 and the β2-adrenergic receptor (β2AR), are sequentially engaged by meningococci to adhere and promote signaling events leading to vascular colonization, but their spatiotemporal coordination is unknown. Here we report that CD147 and β2AR form constitutive hetero-oligomeric complexes. The scaffolding protein alpha-actinin-4 directly binds to the cytosolic tail of CD147 and governs the assembly of CD147/β2AR complexes in highly-ordered clusters at bacterial adhesion sites. This multi-molecular assembly process increases the binding strength of meningococci to endothelial cells under shear stress, and creates molecular platforms for the elongation of membrane protrusions surrounding adherent bacteria. Thus, the specific organization of cellular receptors has major impacts on host-pathogen interaction.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:01:59.788.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sandrine BOURDOULOUS
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-30 01:27:20	ID requested
1	2017-07-10 07:07:51	announced
⏵ 2	2024-10-22 04:02:00	announced	2024-10-22: Updated project metadata.

10.1038/ncomms15764;

Ma, ï, ssa N, Covarelli V, Janel S, Durel B, Simpson N, Bernard SC, Pardo-Lopez L, Bouzinba-S, é, gard H, Faure C, Scott MGH, Coureuil M, Morand PC, Lafont F, Nassif X, Marullo S, Bourdoulous S, -adrenoceptor clusters assembled by alpha-actinin-4. Nat Commun, 8():15764(2017) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: basigin, endothelial cells, Neisseria meningitidis,CD147, nano-LC/MS/MS tandem mass spectrometry

Sandrine BOURDOULOUS
contact affiliation	INSTITUT COCHIN Inserm U1016, CNRS UMR 8104, Université Paris Dsecartes, Sorbonne Paris Cité, France
contact email	sandrine.bourdoulous@inserm.fr
lab head
Sandrine BOURDOULOUS
contact affiliation	Inserm, France
contact email	sandrine.bourdoulous@inserm.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/2017/07/PXD006212

PRIDE project URI

• PRIDE
  1. PXD006212
     1. Label: PRIDE project
     2. Name: Strength of Neisseria meningitidis binding to endothelial cells requires highly-ordered CD147/β2-adrenoceptor clusters assembled by alpha-actinin-4