PXD039002 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | N-glycosite mapping in Brugia malayi female worms, male worms, and microfilariae |
Description | N-linked glycosylation is a critical post translational modification of eukaryotic proteins. N-linked glycans are present on surface and secreted filarial proteins that play a role in host parasite interactions. Examples of glycosylated Brugia malayi proteins have been previously identified but there has not been a systematic study of the N-linked glycoproteome of this or any other filarial parasite. In this study, we applied an enhanced N-glyco FASP protocol using an engineered carbohydrate-binding protein, Fbs1, to enrich N-glycosylated peptides for analysis by LC-MS/MS. We then mapped the N-glycosites on proteins from three host stages of the parasite: adult female, adult male and microfilariae. Fbs1 enrichment of N-glycosylated peptides enhanced the identification of N-glycosites. Our data identified 582 N-linked glycoproteins with 1273 N-glycosites. Gene ontology and cell localization prediction of the identified N-glycoproteins indicated that they were mostly membrane and extracellular proteins. Comparing results from adult female worms, adult male worms, and microfilariae, we find variability in N-glycosylation at the protein level as well as at the individual N-glycosite level. These variations are highlighted in cuticle N-glycoproteins and adult worm restricted N-glycoproteins as examples of proteins at the host parasite interface that are well positioned as potential therapeutic targets or biomarkers. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:59:58.445.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD039002 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Fana Mersha |
SpeciesList | scientific name: Brugia malayi; NCBI TaxID: 6279; |
ModificationList | amidated residue; 2-pyrrolidone-5-carboxylic acid (Gln); acetylated residue; monohydroxylated residue; 1x(18)O labeled deamidated L-asparagine; deamidated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-12-20 20:33:27 | ID requested | |
1 | 2023-04-23 11:03:28 | announced | |
⏵ 2 | 2023-11-14 08:59:58 | announced | 2023-11-14: Updated project metadata. |
Publication List
Keyword List
ProteomeXchange project tag: Biology/Disease-Driven Human Proteome Project (B/D-HPP), Glycoproteomics (B/D-HPP) |
submitter keyword: LC-MSMS, N-glyco FASP,filarial parasite |
Contact List
Jeremy M. Foster |
contact affiliation | Senior Scientist Protein Expression and Modification Division New England Biolabs |
contact email | foster@neb.com |
lab head | |
Fana Mersha |
contact affiliation | New England Biolabs |
contact email | mersha@neb.com |
dataset submitter | |
Full Dataset Link List
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/2023/04/PXD039002 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD039002
- Label: PRIDE project
- Name: N-glycosite mapping in Brugia malayi female worms, male worms, and microfilariae