ArticleeLife2025
The nanoscale organization of the Nipah virus fusion protein informs new membrane fusion mechanisms.
Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.bioRxiv : the preprint server for biology · 2026Article
- Nipah virus preparedness in a One Health framework: Implications for Europe.One health (Amsterdam, Netherlands) · 2026Review
- An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement.Molecular & cellular proteomics : MCP · 2026Article
- Functional and antigenic constraints on the Nipah virus fusion protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026Article
- Functional diversity in GII.4 norovirus entry: HBGA binding and capsid clustering dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding.Science advances · 2025Article
- Single-molecule localisation microscopy approaches reveal envelope glycoprotein clusters in single-enveloped viruses: a potential functional role?Biochemical Society transactions · 2025Review
- Trafficking and Activation ofViruses · 2025Review
- Machine learning assisted in Silico discovery and optimization of small molecule inhibitors targeting the Nipah virus glycoprotein.Scientific reports · 2025Article
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Authors and funding
7 authors.
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Abstract
Paramyxovirus membrane fusion requires an attachment protein for receptor binding and a fusion protein for membrane fusion triggering. Nipah virus (NiV) attachment protein (G) binds to ephrinB2 or -B3 receptors, and fusion protein (F) mediates membrane fusion. NiV-F is a class I fusion protein and is activated by endosomal cleavage. The crystal structure of a soluble GCN4-decorated NiV-F shows a hexamer-of-trimer assembly. Here, we used single-molecule localization microscopy to quantify the NiV-F distribution and organization on cell and virus-like particle membranes at a nanometer precision. We found that NiV-F on biological membranes forms distinctive clusters that are independent of endosomal cleavage or expression levels. The sequestration of NiV-F into dense clusters favors membrane fusion triggering. The nano-distribution and organization of NiV-F are susceptible to mutations at the hexamer-of-trimer interface, and the putative oligomerization motif on the transmembrane domain. We also show that NiV-F nanoclusters are maintained by NiV-F-AP-2 interactions and the clathrin coat assembly. We propose that the organization of NiV-F into nanoclusters facilitates membrane fusion triggering by a mixed population of NiV-F molecules with varied degrees of cleavage and opportunities for interacting with the NiV-G/receptor complex. These observations provide insights into the in situ organization and activation mechanisms of the NiV fusion machinery.
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