ArticlePLoS pathogens2013
Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody.
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 62 papers.
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
62 citing papers in PubMed, 90 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
- 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
- Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein.Virology journal · 2026Article
- Hendra virus: research progress on a bat-borne threat lurking at the human-animal interface.Frontiers in veterinary science · 2026Review
- Antigenic landscape of Nipah virus attachment glycoprotein analysis reveals a protective immunodominant epitope across species.NPJ vaccines · 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
- Single amino acid substitution in Hendra virus attachment glycoprotein induces cross-neutralizing antibodies against Nipah virus.Signal transduction and targeted therapy · 2025Article
- Nipah virus: a summary for clinicians.International journal of emergency medicine · 2025Review
- Nipah virus: pathogenesis, genome, diagnosis, and treatment.Applied microbiology and biotechnology · 2025Review
- 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
- Machine learning assisted in Silico discovery and optimization of small molecule inhibitors targeting the Nipah virus glycoprotein.Scientific reports · 2025Article
- Article
- Henipaviruses: epidemiology, ecology, disease, and the development of vaccines and therapeutics.Clinical microbiology reviews · 2025Review
- Review
- Nipah virus: epidemiology, pathogenesis, treatment, and prevention.Frontiers of medicine · 2024Review
2 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
16 authors at 7 institutions in 2 countries.
Funding
Abstract
The henipaviruses, represented by Hendra (HeV) and Nipah (NiV) viruses are highly pathogenic zoonotic paramyxoviruses with uniquely broad host tropisms responsible for repeated outbreaks in Australia, Southeast Asia, India and Bangladesh. The high morbidity and mortality rates associated with infection and lack of licensed antiviral therapies make the henipaviruses a potential biological threat to humans and livestock. Henipavirus entry is initiated by the attachment of the G envelope glycoprotein to host cell membrane receptors. Previously, henipavirus-neutralizing human monoclonal antibodies (hmAb) have been isolated using the HeV-G glycoprotein and a human naïve antibody library. One cross-reactive and receptor-blocking hmAb (m102.4) was recently demonstrated to be an effective post-exposure therapy in two animal models of NiV and HeV infection, has been used in several people on a compassionate use basis, and is currently in development for use in humans. Here, we report the crystal structure of the complex of HeV-G with m102.3, an m102.4 derivative, and describe NiV and HeV escape mutants. This structure provides detailed insight into the mechanism of HeV and NiV neutralization by m102.4, and serves as a blueprint for further optimization of m102.4 as a therapeutic agent and for the development of entry inhibitors and vaccines.
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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.