PXD062381 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Nipah G glycosylation site provides stability for receptor engagement |
| Description | Nipah virus is a deadly paramyxovirus with 40-75% mortality and >750 cases since 1998. Currently there are no clinically approved vaccines or therapeutics to target infection. Nipah is an enveloped virus with two surface glycoproteins, the trimeric fusion (F) and tetrameric attachment glycoprotein (G). G is responsible for cellular attachment via binding to ephrin B2/B3. Glycosylation of Nipah G and its effects on receptor engagement has not previously been studied but is important as glycosylation impacts immunogenicity, receptor binding and structural conformations for other enveloped virus glycoproteins. Our phylogenetic and mass spectrometry analysis of sitespecific N-glycans of the Nipah G Malaysia strain revealed how N-glycosylation has evolved since the appearance of the virus in 1998. We discovered that the N481 N-glycosite is not conserved and although the glycan does not directly contribute to receptor binding, the threonine/serine in the glycosylation sequon is critical for maintaining long-range stability of individual G subunits that facilitates ephrin B2 binding affinity. Together, these data reveal plasticity of N-glycosylation sites across Nipah species and the presence of hydrogen bonding networks that contribute to G stability and host engagement, which is valuable information for understanding virus attachment/entry mechanisms as well as the rationale design of structure-based vaccines. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-03-30 |
| AnnouncementXML | Submission_2026-03-29_21:54:54.687.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Tia Hawkins |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | monohydroxylated residue; complex glycosylation; deamidated residue; iodoacetamide derivatized residue |
| Instrument | Q Exactive; Synapt MS |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|
| 0 | 2025-03-30 10:49:11 | ID requested | |
| ⏵ 1 | 2026-03-29 21:54:55 | announced | |
Publication List
| Hawkins T É, Calvaresi V, Burnap SA, Demyanenko Y, Wu L, Struwe WB, An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement. Mol Cell Proteomics, 25(4):101531(2026) [pubmed] |
| 10.1016/j.mcpro.2026.101531; |
Keyword List
Contact List
| Weston Struwe |
|---|
| contact affiliation | Biochemistry Department, Kavli Institute for Nanoscience Discovery, University of Oxford, UK |
| contact email | weston.struwe@bioch.ox.ac.uk |
| lab head | |
| Tia Hawkins |
|---|
| contact affiliation | The Rosalind Franklin Institute & University of Oxford |
| contact email | tia.hawkins@chem.ox.ac.uk |
| 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/2026/03/PXD062381 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD062381
- Label: PRIDE project
- Name: Nipah G glycosylation site provides stability for receptor engagement
