ArticleCell2020
Potent Henipavirus Neutralization by Antibodies Recognizing Diverse Sites on Hendra and Nipah Virus Receptor Binding Protein.
Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
54 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Therapeutics for Nipah virus disease: a systematic review to support prioritisation of drug candidates for clinical trials.The Lancet. Microbe · 2025Pooled it
- Review
- Computational design of potent, broadly neutralizing anti-Nipah virus and Hendra virus miniproteins.bioRxiv : the preprint server for biology · 2026Article
- Nipah Virus: A Neurotropic Zoonosis-From Molecular Biology to Clinical Manifestations and Translational Advances.Viruses · 2026Review
- Cross-clade vaccination to overcome sarbecovirus or merbecovirus neutralization gaps.Cell reports · 2026Article
- Mechanistic and antigenic boundaries of Henipavirus and Parahenipavirus glycoproteins.Nature communications · 2026Article
- Article
- Three decades of discovery: An overview of Hendra virus, the original Henipavirus.PLoS neglected tropical diseases · 2026Review
- Oral 4'fluorouridine provides postexposure protection against lethal Nipah virus infection.bioRxiv : the preprint server for biology · 2026Article
- Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein.Virology journal · 2026Article
- A risk-gate mechanistic-ecological framework for assessing emergence potential of henipa-related viruses.Frontiers in microbiology · 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
- 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
- Article
- Laboratory Diagnosis of Hendra and Nipah: Two Emerging Zoonotic Diseases with One Health Significance.Viruses · 2025Review
- Characterization of an mRNA-Encoded Antibody Against Henipavirus.Current issues in molecular biology · 2025Article
- Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A Highly Specific Antibody-Based Assay forViruses · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
Hendra (HeV) and Nipah (NiV) viruses are emerging zoonotic pathogens in the Henipavirus genus causing outbreaks of disease with very high case fatality rates. Here, we report the first naturally occurring human monoclonal antibodies (mAbs) against HeV receptor binding protein (RBP). All isolated mAbs neutralized HeV, and some also neutralized NiV. Epitope binning experiments identified five major antigenic sites on HeV-RBP. Animal studies demonstrated that the most potent cross-reactive neutralizing mAbs, HENV-26 and HENV-32, protected ferrets in lethal models of infection with NiV Bangladesh 3 days after exposure. We solved the crystal structures of mAb HENV-26 in complex with both HeV-RBP and NiV-RBP and of mAb HENV-32 in complex with HeV-RBP. The studies reveal diverse sites of vulnerability on RBP recognized by potent human mAbs that inhibit virus by multiple mechanisms. These studies identify promising prophylactic antibodies and define protective epitopes that can be used in rational vaccine design.
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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.