PXD051707 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Dual functional POGases Encompassing O-glycanase and Adhesin Activities |
Description | Mucin-type O-glycans on glycoproteins play many pivotal roles in biological processes, making O-glycosylation of biotherapeutics a potential critical quality attribute. Defining the structurefunction relationship of O-glycans is hindered by the lack of enzymatic tools to release all complex O-glycans from glycoproteins. Furthermore, glycans on host cells often serve as ligands for lectins/adhesins on bacteria for bacterium-host interactions, which are essential for the colonization of commensal bacteria and attachment/invasion of pathogens. More emerging adhesins require identification and characterization. To identify endo-α-Nacetylgalactosaminidases (O-glycanases, GH101) with broad substrate specificities, termed Peptide:O-Glycosidase (POGase), we screened putative candidates from 46 different bacteria with fluorogenic α2,3sialylCore 1 substrates, identified five POGase orthologs, and characterized one that releases sialylated complex O-glycans from glycopeptides, glycoproteins and biotherapeutics. Three unique peptide motifs differentiate the POGase existing in phylum Actinomycetota from known O-glycanases. Furthermore, while the POGases contain the GH101 domain, other domains at the C-terminus are required for efficient O-glycanase activity and possess binding activity to major glycans commonly decorating epithelial cells. The dual function POGases, which encompass O-glycanase and adhesin activities, will shed light on O-glycomics, quality assessment of O-glycoprotein drugs, microbiology, and pathogenesis of diseases that may lead to novel therapeutics. |
HostingRepository | PRIDE |
AnnounceDate | 2025-02-25 |
AnnouncementXML | Submission_2025-02-25_08:06:57.043.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | John Bettinger |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | complex glycosylation |
Instrument | ultraflex; Synapt MS |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-04-24 09:41:54 | ID requested | |
⏵ 1 | 2025-02-25 08:06:57 | announced | |
Publication List
Keyword List
submitter keyword: enzyme, glycopeptides,O-glycans |
Contact List
Tongzhong Ju |
contact affiliation | FDA |
contact email | tongzhong.ju@fda.hhs.gov |
lab head | |
John Bettinger |
contact affiliation | FDA |
contact email | john.bettinger@fda.hhs.gov |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD051707
- Label: PRIDE project
- Name: Dual functional POGases Encompassing O-glycanase and Adhesin Activities