PXD028437

PXD028437 is an original dataset announced via ProteomeXchange.

Title	Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens
Description	Mechanisms of infection and pathogenesis have predominantly been studied based on differential gene or protein expression. Less is known about posttranslational modifications, which are essential for protein functional diversity. We applied an innovative glycoproteomics method to study the systemic proteome-wide glycosylation in response to infection. The protein site-specific glycosylation was characterized in plasma derived from well-defined controls and patients. We found 3862 unique features, of which we identified 463 distinct intact glycopeptides, that could be mapped to more than 30 different proteins. Statistical analyses were used to derive a glycopeptide signature that enabled significant differentiation between patients with a bacterial or viral infection. Furthermore, supported by a machine learning algorithm, we demonstrated the ability to identify the causative pathogens based on the distinctive host blood plasma glycopeptide signatures. These results illustrate that glycoproteomics holds enormous potential as an innovative approach to improve the interpretation of relevant biological changes in response to infection.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_07:13:28.608.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Esther Willems
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	maXis

Revision	Datetime	Status	ChangeLog Entry
0	2021-09-09 13:54:33	ID requested
1	2023-07-17 23:13:45	announced
⏵ 2	2023-11-14 07:13:29	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

submitter keyword: glycoproteomics, mass spectrometry, site specific glycosylation, infectious disease, α1-acid glycoprotein (AGP), intact glycopeptides, biomarker

Prof. Alain van Gool
contact affiliation	Translational Metabolic Laboratory, Department of Laboratory Medicine, Radboud Institute for Molecular Life Sciences, Radboud university medical center, Nijmegen, The Netherlands
contact email	alain.vangool@radboudumc.nl
lab head
Esther Willems
contact affiliation	Radboudumc
contact email	esther.willems1@radboudumc.nl
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/2023/07/PXD028437

PRIDE project URI

• PRIDE
  1. PXD028437
     1. Label: PRIDE project
     2. Name: Impact of infection on proteome-wide glycosylation revealed by distinct signatures for bacterial and viral pathogens