ArticleNature structural & molecular biology2019
An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
What it found
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Who cites it
78 citing papers in PubMed, 116 citations in OpenAlex.
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- A single-cycle, recombinant VSV platform Nipah vaccine cross-protects against Hendra virus in nonhuman primates.PLoS pathogens · 2026Article
- Pre-Cambrian origin ofeLife · 2026Article
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.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
- The Silent Spillover Threat: Nipah Virus Epidemiology, Pathogenesis, Clinical Manifestations, and Advances in Therapeutics and Vaccine Development.Microorganisms · 2026Review
- Three decades of discovery: An overview of Hendra virus, the original Henipavirus.PLoS neglected tropical diseases · 2026Review
- 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
- Cloning, expression and characterisation of antigen-specific recombinant bat immunoglobulin from the black flying fox (Frontiers in immunology · 2026Article
- Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species.NPJ vaccines · 2025Article
- Nipah Virus Inhibitor Knowledgebase (NVIK): a combined evidence approach to prioritise small molecule inhibitors.Journal of cheminformatics · 2025Article
- A nanobody-based therapeutic targeting Nipah virus limits viral escape.Nature structural & molecular biology · 2025Article
- Antigenic and structural insights into Langya henipavirus attachment glycoprotein.Virologica Sinica · 2025Article
- Establishment of a Pseudovirus-Based Golden Hamster Model for the Attachment and Entry Stages of Hendra Virus Infection and Evaluation of Protective Immunity.Pathogens (Basel, Switzerland) · 2025Article
- Review
- Single amino acid substitution in Hendra virus attachment glycoprotein induces cross-neutralizing antibodies against Nipah virus.Signal transduction and targeted therapy · 2025Article
- Characterization of an mRNA-Encoded Antibody Against Henipavirus.Current issues in molecular biology · 2025Article
- Nipah virus: pathogenesis, genome, diagnosis, and treatment.Applied microbiology and biotechnology · 2025Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
Abstract
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness with fatality rates of 50-100%. No vaccines or licensed therapeutics currently exist to protect humans against NiV or HeV. HNVs enter host cells by fusing the viral and cellular membranes via the concerted action of the attachment (G) and fusion (F) glycoproteins, the main targets of the humoral immune response. Here, we describe the isolation and humanization of a potent monoclonal antibody cross-neutralizing NiV and HeV. Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. This work supports the importance of the HNV prefusion F conformation for eliciting a robust immune response and paves the way for using this antibody for prophylaxis and post-exposure therapy with NiV- and HeV-infected individuals.
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Registered trials
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.