ArticleScience (New York, N.Y.)2022
Architecture and antigenicity of the Nipah virus attachment glycoprotein.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
59 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- Pan-neutralization of parainfluenza viruses by a hemagglutinin-neuraminidase antibody.bioRxiv : the preprint server for biology · 2026Article
- Cryo-electron tomography of Nipah virus structural protein complexes in virus-like particles.bioRxiv : the preprint server for biology · 2026Article
- NSUN2‑mediated epitranscriptomic and ubiquitin modulation of Nipah virus matrix protein reveals a dual-targeting antiviral strategy.Protein & cell · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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
- Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein.Virology journal · 2026Article
- Computational design of immunogenic peptide-ligand conjugates for targeted therapy against Nipah virus infection.Frontiers in bioinformatics · 2026Article
- Functional and antigenic constraints on the Nipah virus fusion protein.bioRxiv : the preprint server for biology · 2026Article
- 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
- Review
- Single amino acid substitution in Hendra virus attachment glycoprotein induces cross-neutralizing antibodies against Nipah virus.Signal transduction and targeted therapy · 2025Article
- Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structural biology of Nipah virus G and F glycoproteins: Insights into therapeutic and vaccine development.European journal of microbiology & immunology · 2025Review
- Strain-Divergent m6A Landscapes Modulate Nipah Virus Replication and METTL3 Inhibition Attenuates Virulence.Viruses · 2025Article
- A Highly Specific Antibody-Based Assay forViruses · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness. The entry of HNVs into host cells requires the attachment (G) and fusion (F) glycoproteins, which are the main targets of antibody responses. To understand viral infection and host immunity, we determined a cryo-electron microscopy structure of the NiV G homotetrameric ectodomain in complex with the nAH1.3 broadly neutralizing antibody Fab fragment. We show that a cocktail of two nonoverlapping G-specific antibodies neutralizes NiV and HeV synergistically and limits the emergence of escape mutants. Analysis of polyclonal serum antibody responses elicited by vaccination of macaques with NiV G indicates that the receptor binding head domain is immunodominant. These results pave the way for implementing multipronged therapeutic strategies against these deadly pathogens.
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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.