PXD007037 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccines |
Description | The outbreak of a pandemic influenza H1N1 in 2009 required the rapid generation of high-yielding vaccines against the A/California/7/2009 virus, which were achieved by either addition or deletion of a glycosylation site in the influenza proteins hemagglutinin and neuraminidase. In this report, we have systematically evaluated the glycan composition, structural distribution and topology of glycosylation for two high-yield candidate reassortant vaccines (NIBRG-121xp and NYMC-X181A) by combining various enzymatic digestions with high performance liquid chromatography and multiple-stage mass spectrometry. Proteomic data analyses of the full-length protein sequences determined 9 N-glycosylation sites of hemagglutinin, and defined 6 N-glycosylation sites and the glycan structures of low abundance neuraminidase, which were occupied by high-mannose, hybrid and complex-type N-glycans. A total of ~300 glycopeptides were analyzed and manually validated by tandem mass spectrometry. The unique N-glycan structure and topological location of these N-glycans are highly correlated to the spatial protein structure and the residential ligand binding. Interestingly, sulfation, fucosylation and bisecting N-acetylglucosamine of N-glycans were also reliably identified at the specific glycosylation sites of the two influenza proteins that may serve a crucial role in regulating the protein structure and increasing the protein abundance of the influenza virus reassortants. |
HostingRepository | PRIDE |
AnnounceDate | 2018-11-21 |
AnnouncementXML | Submission_2018-11-21_08:02:18.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Yi-Min She |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue; deamidated residue |
Instrument | LTQ FT |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-07-13 07:59:17 | ID requested | |
⏵ 1 | 2018-11-21 08:02:19 | announced | |
Publication List
She YM, Farnsworth A, Li X, Cyr TD, Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccines. Sci Rep, 7(1):10232(2017) [pubmed] |
Keyword List
ProteomeXchange project tag: Biology/Disease-Driven Human Proteome Project (B/D-HPP), Human Proteome Project, Glycoproteomics (B/D-HPP) |
submitter keyword: Influenza H1N1, LC MS/MS |
Contact List
Terry Cyr |
contact affiliation | Centre for Biologics Evaluation, Biologics and Genetic Therapies Directorate, Health Canada, Canada |
contact email | terry.cyr@hc-sc.gc.ca |
lab head | |
Yi-Min She |
contact affiliation | Health Canada |
contact email | yi-min.she@hc-sc.gc.ca |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD007037
- Label: PRIDE project
- Name: Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccines