ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure and stabilization of the Hendra virus F glycoprotein in its prefusion form.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.
- 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
- Highly potent C-type nanoantibodies neutralize Nipah and Hendra viruses by cavity filling on fusion glycoprotein.Nature communications · 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
- 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
- Rabies virus-vectored Lyme disease vaccine provides long-term protection against tick-transmitted Borrelia burgdorferi.NPJ vaccines · 2025Article
- Broad-spectrum vaccines against various and evolving viruses: from antigen design to nanoparticle delivery.Journal of virology · 2025Review
- Potent Cross-neutralizing Antibodies Reveal Vulnerabilities of Henipavirus Fusion Glycoprotein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A monoclonal antibody targeting the Nipah virus fusion glycoprotein apex imparts protection from disease.Journal of virology · 2024Article
- Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein.Nature communications · 2024Article
- Structure and design of Langya virus glycoprotein antigens.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Prefusion stabilization of the Hendra and Langya virus F proteins.Journal of virology · 2024Article
- A general computational design strategy for stabilizing viral class I fusion proteins.Nature communications · 2024Article
- Systematic computer-aided disulfide design as a general strategy to stabilize prefusion class I fusion proteins.Frontiers in immunology · 2024Article
- Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes.Life science alliance · 2023Article
- Structure and design of Langya virus glycoprotein antigens.bioRxiv : the preprint server for biology · 2023Article
- Structures of Langya Virus Fusion Protein Ectodomain in Pre- and Postfusion Conformation.Journal of virology · 2023Article
- Structure and antigenicity of divergent Henipavirus fusion glycoproteins.Nature communications · 2023Article
- Review
- Potent monoclonal antibody-mediated neutralization of a divergent Hendra virus variant.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Hendra virus (HeV) is one of the two prototypical members of the Henipavirus genus of paramyxoviruses, which are designated biosafety level 4 (BSL-4) organisms due to the high mortality rate of Nipah virus (NiV) and HeV in humans. Paramyxovirus cell entry is mediated by the fusion protein, F, in response to binding of a host receptor by the attachment protein. During posttranslational processing, the fusion peptide of F is released and, upon receptor-induced triggering, inserts into the host cell membrane. As F undergoes a dramatic refolding from its prefusion to postfusion conformation, the fusion peptide brings the host and viral membranes together, allowing entry of the viral RNA. Here, we present the crystal structure of the prefusion form of the HeV F ectodomain. The structure shows very high similarity to the structure of prefusion parainfluenza virus 5 (PIV5) F, with the main structural differences in the membrane distal apical loops and the fusion peptide cleavage loop. Functional assays of mutants show that the apical loop can tolerate perturbation in length and surface residues without loss of function, except for residues involved in the stability and conservation of the F protein fold. Structure-based disulfide mutants were designed to anchor the fusion peptide to conformationally invariant residues of the F head. Two mutants were identified that inhibit F-mediated fusion by stabilizing F in its prefusion conformation.
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