PXD007895 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-10-03 01:35:13 | ID requested | |
⏵ 1 | 2022-02-28 03:54:59 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
curator keyword: Technical |
submitter keyword: O-linked glycoproteomics, site specific, solid phase, HIV |
Contact List
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 | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD007895
- Label: PRIDE project
- Name: Site-specific Analysis of O-linked Glycoproteome Using Chemoenzymatic Strategy, part 2