PXD009676

PXD009676 is an original dataset announced via ProteomeXchange.

Title	Ample glycosylation in membrane and cell envelope protein explains phenotypic diversity, virulence and AMR in the Mycobacterium tuberculosis complex
Description	Glycoproteomics is likely to identify Mtb virulence factors because glycoproteins on the bacterial cell envelope are used by mycobacteria to enter the primary human host cell, the macrophage. It has been proposed that Mtb interacts with mannose receptors on host cells via mannosylated proteins to enter the macrophages. Despite the vital importance of these proteins in Mtb pathogenesis, our current knowledge of Mtb glycoproteins is still limited, and only a few secreted and cell wall-associated glycoproteins have to date been described. Previous studies have used laboratory strains as model systems to study glycosylation in Mtb. However, only a few sub-groups within the genetically conserved MTBC appear to cause extensive outbreaks with different clinical presentation and AMR. In this study, we employed qualitative and quantitative mass spectrometry and bioinformatics to explore the glycoproteomic patterns of clinical isolates from four lineages of the MTBC, lineages 3, 4, 5 and 7, to investigate the role of protein glycosylation in Mtb adaptation, survival and AMR.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:44:51.562.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alemayehu Godana Birhanu
SpeciesList	scientific name: Mycobacterium tuberculosis H37Rv; NCBI TaxID: 83332;
ModificationList	complex glycosylation
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-04 05:34:13	ID requested
1	2019-03-25 10:03:22	announced
⏵ 2	2024-10-22 04:44:52	announced	2024-10-22: Updated project metadata.

Birhanu AG, Yimer SA, Kalayou S, Riaz T, Zegeye ED, Holm-Hansen C, Norheim G, Aseffa A, Abebe M, T, ø, njum T, Ample glycosylation in membrane and cell envelope proteins may explain the phenotypic diversity and virulence in the Mycobacterium tuberculosis complex. Sci Rep, 9(1):2927(2019) [pubmed]

10.1038/s41598-019-39654-9;

curator keyword: Biological

submitter keyword: glycosylation, phenotypic variability, PTMs, virulence, glycoproteomics,M. tuberculosis

Alemayehu Godana Birhanu
contact affiliation	University of Oslo Faculty of Medicine Department of Microbiology
contact email	a.g.birhanu@studmed.uio.no
lab head
Alemayehu Godana Birhanu
contact affiliation	PhD candidate, Faculty of Medicine, University of Oslo, Norway
contact email	alexbiology97@yahoo.com
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/2019/03/PXD009676

PRIDE project URI

• PRIDE
  1. PXD009676
     1. Label: PRIDE project
     2. Name: Ample glycosylation in membrane and cell envelope protein explains phenotypic diversity, virulence and AMR in the Mycobacterium tuberculosis complex