ArticleProceedings of the National Academy of Sciences of the United States of America2019
A structural basis for antibody-mediated neutralization of Nipah virus reveals a site of vulnerability at the fusion glycoprotein apex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 75 citations in OpenAlex.
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Highly potent C-type nanoantibodies neutralize Nipah and Hendra viruses by cavity filling on fusion glycoprotein.Nature communications · 2026Article
- Systematic multi-reference vertebrate ACE2 sequence similarity analysis predicts species susceptibility to SARS-related sarbecoviruses.Scientific reports · 2026Article
- Purification and immunogenicity of Nipah virus-like particles from insect cells.BMC biotechnology · 2025Article
- Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species.NPJ vaccines · 2025Article
- Antigenic and structural insights into Langya henipavirus attachment glycoprotein.Virologica Sinica · 2025Article
- A nanobody-based therapeutic targeting Nipah virus limits viral escape.Nature structural & molecular biology · 2025Article
- Single amino acid substitution in Hendra virus attachment glycoprotein induces cross-neutralizing antibodies against Nipah virus.Signal transduction and targeted therapy · 2025Article
- A second-generation molecular clamp stabilised bivalent candidate vaccine for protection against diseases caused by respiratory syncytial virus and human metapneumovirus.PLoS pathogens · 2025Article
- Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Single-molecule localisation microscopy approaches reveal envelope glycoprotein clusters in single-enveloped viruses: a potential functional role?Biochemical Society transactions · 2025Review
- Structural biology of Nipah virus G and F glycoproteins: Insights into therapeutic and vaccine development.European journal of microbiology & immunology · 2025Review
- From antibiotic to antiviral: computational screening reveals a multi-targeting antibiotic from Streptomyces spp. against Nipah virus fusion proteins.Molecular diversity · 2025Article
- An Updated Review on Nipah Virus Infection with a Focus on Encephalitis, Vasculitis, and Therapeutic Approaches.Current topics in medicinal chemistry · 2025Review
- A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease.Journal of virology · 2024Article
- A neutralizing antibody prevents postfusion transition of measles virus fusion protein.Science (New York, N.Y.) · 2024Article
- High allelic diversity in Arabidopsis NLRs is associated with distinct genomic features.EMBO reports · 2024Article
- Structure and design of Langya virus glycoprotein antigens.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structure-guided mutagenesis of Henipavirus receptor-binding proteins reveals molecular determinants of receptor usage and antibody-binding epitopes.Journal of virology · 2024Article
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Authors and funding
14 authors at 7 institutions in 2 countries.
Funding
Abstract
Nipah virus (NiV) is a highly pathogenic paramyxovirus that causes frequent outbreaks of severe neurologic and respiratory disease in humans with high case fatality rates. The 2 glycoproteins displayed on the surface of the virus, NiV-G and NiV-F, mediate host-cell attachment and membrane fusion, respectively, and are targets of the host antibody response. Here, we provide a molecular basis for neutralization of NiV through antibody-mediated targeting of NiV-F. Structural characterization of a neutralizing antibody (nAb) in complex with trimeric prefusion NiV-F reveals an epitope at the membrane-distal domain III (DIII) of the molecule, a region that undergoes substantial refolding during host-cell entry. The epitope of this monoclonal antibody (mAb66) is primarily protein-specific and we observe that glycosylation at the periphery of the interface likely does not inhibit mAb66 binding to NiV-F. Further characterization reveals that a Hendra virus-F-specific nAb (mAb36) and many antibodies in an antihenipavirus-F polyclonal antibody mixture (pAb835) also target this region of the molecule. Integrated with previously reported paramyxovirus F-nAb structures, these data support a model whereby the membrane-distal region of the F protein is targeted by the antibody-mediated immune response across henipaviruses. Notably, our domain-specific sequence analysis reveals no evidence of selective pressure at this region of the molecule, suggestive that functional constraints prevent immune-driven sequence variation. Combined, our data reveal the membrane-distal region of NiV-F as a site of vulnerability on the NiV surface.
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