An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement.

Tia É Hawkins, Valeria Calvaresi, Sean A Burnap, Yana Demyanenko, Liang Wu, Weston B Struwe

Abstract read

In one paragraph

Article in Molecular & cellular proteomics : MCP, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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3 · Its place in the literature

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1 citing paper in PubMed.

Antigenic and mutational insights into the Nipah virus G glycoprotein: implications for viral entry, host specificity, therapeutics, and vaccine development.PeerJ · 2025
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5 · Who and what money

Authors and funding

6 authors.

Tia É HawkinsThe Rosalind Franklin Institute, Harwell Science & Innovation Campus, Harwell, UK; Kavli Institute for Nanoscience Discovery, University of Oxford, UK; Department of Chemistry, University of Oxford, Oxford, UK.

Valeria CalvaresiKavli Institute for Nanoscience Discovery, University of Oxford, UK; Department of Biochemistry, University of Oxford, Oxford, UK.

Sean A BurnapKavli Institute for Nanoscience Discovery, University of Oxford, UK; Department of Biochemistry, University of Oxford, Oxford, UK.

Yana DemyanenkoThe Rosalind Franklin Institute, Harwell Science & Innovation Campus, Harwell, UK.

Liang WuThe Rosalind Franklin Institute, Harwell Science & Innovation Campus, Harwell, UK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, Oxford, UK. Electronic address: liang.wu@rfi.ac.uk.

Weston B StruweKavli Institute for Nanoscience Discovery, University of Oxford, UK; Department of Biochemistry, University of Oxford, Oxford, UK. Electronic address: weston.struwe@bioch.ox.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nipah virus is a deadly paramyxovirus with 40 to 75% mortality and >750 cases since 1998. Currently there are no clinically approved vaccines or therapeutics to treat infection. Nipah is an enveloped virus with two surface glycoproteins, the trimeric fusion glycoprotein (F), and the tetrameric attachment glycoprotein (G), which is responsible for cellular attachment via binding to the host ephrin B2/B3 receptor. Glycosylation can substantially affect immunogenicity, receptor binding, and structural conformations for virus glycoproteins, but its effects on Nipah G receptor engagement have not been studied. Here, phylogenetic and mass spectrometry analysis of the Nipah G Malaysia strain reveal how N-glycosylation has evolved since the appearance of the virus in 1998. We discovered that the N481 sequon is not conserved and the threonine/serine in the glycosylation site is critical for maintaining long-range stability of 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-results that are valuable for understanding virus attachment/entry mechanisms and the rational design of structure-based vaccines.

Indexed as

Evolution, MolecularNipah VirusViral Envelope ProteinsAmino Acid SequenceEphrin-B2GlycosylationHumansPhylogenyProtein BindingEphrin-B2Viral Envelope Proteinsattachment glycoprotein (G)Ephrin B2Nipah virussite-specific glycan Astructural dynamics

Identifiers

PMID41713789

DOI10.1016/j.mcpro.2026.101531

PMCPMC13020074

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.