PXD007895

PXD007895 is an original dataset announced via ProteomeXchange.

Title	Site-specific Analysis of O-linked Glycoproteome Using Chemoenzymatic Strategy, part 2
Description	Protein glycosylation is ubiquitous and plays critical roles in biology. However, study of O-linked glycoproteome (O-glycoproteome), a major type of protein glycosylation, has been severely impeded due to paucity of technology. We presented a chemoenzymatic strategy for extraction of site-specific O-linked glycopeptides (SOGO), which enabled simultaneous enrichment and identification of O-linked glycosylation sites (O-glycosites) in an unprecedented depth. Central to SOGO is a tandem-use of solid-phase capture of peptides and an O-linked glycan (O-glycan) dependent endoprotease named OpeRATOR. Interestingly, OpeRATOR requires O-glycan to specifically cleave the N-terminus of glycan-occupied Ser and Thr leading to unambiguous identification of O-glycosites and corresponding glycoproteins. The identified O-glycosites facilitated downstream determination of microheterogeneity of intact O-linked glycopeptides (O-glycopeptides). We benchmarked the method using human serum and identified 805 peptides containing 777 O-glycosites from 1,345 site-specific O-glycopeptides and 302 glycoproteins. We applied the method to study change of protein-specific O-glycosylation in human T cells infected with human immunodeficiency virus (HIV-1). Strikingly, 1404 peptides containing 1,352 O-glycosites from 577 glycoproteins were identified. In addition, altered site-specific O-linked glycosylation (O-glycosylation) during HIV infection of T cells were observed. In total, 1989 O-glycosites from 789 glycoproteins were precisely pinpointed from human serum and T cells. We observed conserved motifs for O-glycoproteome. Finally, ontology analysis revealed diverse roles for O-glycoproteins arguing broad application of our method to study biology in respective to protein O-glycosylation.
HostingRepository	PRIDE
AnnounceDate	2022-02-28
AnnouncementXML	Submission_2022-02-28_03:54:59.599.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Weiming Yang
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	L-homoarginine; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-10-03 01:35:13	ID requested
⏵ 1	2022-02-28 03:54:59	announced

Dataset with its publication pending

curator keyword: Technical

submitter keyword: O-linked glycoproteomics, site specific, solid phase, HIV

Hui Zhang
contact affiliation	Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
contact email	huizhang@jhu.edu
lab head
Weiming Yang
contact affiliation	Johns Hopkins University
contact email	wesley.young@hotmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD007895
     1. Label: PRIDE project
     2. Name: Site-specific Analysis of O-linked Glycoproteome Using Chemoenzymatic Strategy, part 2