ArticleNature communications2024
Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- A highly potent, stable, and safe dePEGylated lipopeptide against Nipah virus and related henipaviruses.Emerging microbes & infections · 2026Article
- A shark variable new antigen receptor recognizes an occluded epitope of fibroblast activation protein.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
- Highly potent C-type nanoantibodies neutralize Nipah and Hendra viruses by cavity filling on fusion glycoprotein.Nature communications · 2026Article
- Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein.Virology journal · 2026Article
- Engineering Nipah virus: Reverse genetics as a gateway to novel drug discovery.New microbes and new infections · 2026Review
- 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
- Identification of a Highly Potent Neutralizing Nanobody Against Human Adenovirus Type 4.Vaccines · 2025Article
- Article
- Self-assembled nanoparticle vaccine comprised of multiple epitopes provides robust protective immunity against reoviruses in fish model.Cell communication and signaling : CCS · 2025Article
- Trends in nanobody radiotheranostics.European journal of nuclear medicine and molecular imaging · 2025Review
- Highly Potent Neutralizing Nanobodies Acting Against Chikungunya Virus Infection via Inhibiting Multiple Stages of the Viral Life Cycle.International journal of molecular sciences · 2025Article
- Review
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Authors and funding
19 authors.
Funding
Abstract
Nipah virus infection, one of the top priority diseases recognized by the World Health Organization, underscores the urgent need to develop effective countermeasures against potential epidemics and pandemics. Here, we identify a fully human single-domain antibody that targets a highly conserved cryptic epitope situated at the dimeric interface of the Nipah virus G protein (receptor binding protein, RBP), as elucidated through structures by high-resolution cryo-electron microscopy (cryo-EM). This unique binding mode disrupts the tetramerization of the G protein, consequently obstructing the activation of the F protein and inhibiting viral membrane fusion. Furthermore, our investigations reveal that this compact antibody displays enhanced permeability across the blood-brain barrier (BBB) and demonstrates superior efficacy in eliminating pseudovirus within the brain in a murine model of Nipah virus infection, particularly compared to the well-characterized antibody m102.4 in an IgG1 format. Consequently, this single-domain antibody holds promise as a therapeutic candidate to prevent Nipah virus infections and has potential implications for vaccine development.
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