PXD062381

PXD062381 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2025-03-30 10:49:11	ID requested
⏵ 1	2026-03-29 21:54:55	announced

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;

submitter keyword: None

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

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PRIDE project URI

• PRIDE
  1. PXD062381
     1. Label: PRIDE project
     2. Name: Nipah G glycosylation site provides stability for receptor engagement