ArticlePLoS pathogens2013
Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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Who cites it
95 citing papers in PubMed.
- A highly potent, stable, and safe dePEGylated lipopeptide against Nipah virus and related henipaviruses.Emerging microbes & infections · 2026Article
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- Assessing the pandemic potential of Nipah virus: From molecular pathogenesis to ecological spillover risks.Infectious medicine · 2026Review
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.bioRxiv : the preprint server for biology · 2026Article
- Genotype IX Newcastle disease virus isolated from wild birds is attenuated by hemagglutinin-neuraminidase mutation.Journal of virology · 2026Article
- An Evolutionary Distinct Nipah Virus N-Glycosylation Site Provides Stability for Receptor Engagement.Molecular & cellular proteomics : MCP · 2026Article
- Nipah virus on the radar: The choice to catch early or catch up later.New microbes and new infections · 2026Article
- Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein.Virology journal · 2026Article
- Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species.NPJ vaccines · 2025Article
- Efficient in vivo generation of CAR T cells using a retargeted fourth-generation lentiviral vector.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design.ACS nano · 2025Article
- Article
- From antibiotic to antiviral: computational screening reveals a multi-targeting antibiotic from Streptomyces spp. against Nipah virus fusion proteins.Molecular diversity · 2025Article
- Multi-platform omics analysis of Nipah virus infection reveals viral glycoprotein modulation of mitochondria.Cell reports · 2025Article
- Henipaviruses: epidemiology, ecology, disease, and the development of vaccines and therapeutics.Clinical microbiology reviews · 2025Review
- Flow virometry: recent advancements, best practices, and future frontiers.Journal of virology · 2025Review
- Article
- The nanoscale organization of the Nipah virus fusion protein informs new membrane fusion mechanisms.eLife · 2025Article
- An attachment glycoprotein nanoparticle elicits broadly neutralizing antibodies and protects against lethal Nipah virus infection.NPJ vaccines · 2024Article
35 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Membrane fusion is essential for entry of the biomedically-important paramyxoviruses into their host cells (viral-cell fusion), and for syncytia formation (cell-cell fusion), often induced by paramyxoviral infections [e.g. those of the deadly Nipah virus (NiV)]. For most paramyxoviruses, membrane fusion requires two viral glycoproteins. Upon receptor binding, the attachment glycoprotein (HN/H/G) triggers the fusion glycoprotein (F) to undergo conformational changes that merge viral and/or cell membranes. However, a significant knowledge gap remains on how HN/H/G couples cell receptor binding to F-triggering. Via interdisciplinary approaches we report the first comprehensive mechanism of NiV membrane fusion triggering, involving three spatiotemporally sequential cell receptor-induced conformational steps in NiV-G: two in the head and one in the stalk. Interestingly, a headless NiV-G mutant was able to trigger NiV-F, and the two head conformational steps were required for the exposure of the stalk domain. Moreover, the headless NiV-G prematurely triggered NiV-F on virions, indicating that the NiV-G head prevents premature triggering of NiV-F on virions by concealing a F-triggering stalk domain until the correct time and place: receptor-binding. Based on these and recent paramyxovirus findings, we present a comprehensive and fundamentally conserved mechanistic model of paramyxovirus membrane fusion triggering and cell entry.
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