ArticleJournal of virology2006
Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 53 citations in OpenAlex.
- Discovery of Quercetin as a Potential Entry Inhibitor of Nipah Virus: A Path Toward Antiviral Therapy.International journal of molecular sciences · 2026Article
- Machine learning-driven drug repurposing and computational validation for Nipah virus.Molecular diversity · 2026Article
- Ephrin B2 and Ephrin B3 are receptors for a novel putative henipavirus with zoonotic potential.PLoS neglected tropical diseases · 2026Article
- The Nipah virus threat in India: Epidemiological trends, risk drivers, and lessons for pandemic preparedness.PLoS pathogens · 2026Review
- Computational design of immunogenic peptide-ligand conjugates for targeted therapy against Nipah virus infection.Frontiers in bioinformatics · 2026Article
- Nipah virus: pathogenesis, genome, diagnosis, and treatment.Applied microbiology and biotechnology · 2025Review
- Review
- Structure-guided mutagenesis of Henipavirus receptor-binding proteins reveals molecular determinants of receptor usage and antibody-binding epitopes.Journal of virology · 2024Article
- Genomic characterization, transcriptome analysis, and pathogenicity of the Nipah virus (Indian isolate).Virulence · 2023Article
- Nipah Virus: An Overview of the Current Status of Diagnostics and Their Role in Preparedness in Endemic Countries.Viruses · 2023Review
- A Survey of Henipavirus Tropism-Our Current Understanding from a Species/Organ and Cellular Level.Viruses · 2023Review
- Advancing the frontiers: Revolutionary control and prevention paradigms against Nipah virus.Open veterinary journal · 2023Review
- Discovery and Genomic Characterization of a Novel Henipavirus, Angavokely Virus, from Fruit Bats in Madagascar.Journal of virology · 2022Article
- Glycoprotein attachment with host cell surface receptor ephrin B2 and B3 in mediating entry of nipah and hendra virus: a computational investigation.Journal of chemical sciences (Bangalore, India) · 2022Article
- Antivirals targeting paramyxovirus membrane fusion.Current opinion in virology · 2021Review
- Evolution of Nipah Virus Infection: Past, Present, and Future Considerations.Tropical medicine and infectious disease · 2021Review
- High Pathogenicity of Nipah Virus from Pteropus lylei Fruit Bats, Cambodia.Emerging infectious diseases · 2020Article
- Roles of the highly conserved amino acids in the second receptor binding site of the Newcastle disease virus HN protein.Virology journal · 2019Article
- Nano-based approach to combat emerging viral (NIPAH virus) infection.Nanomedicine : nanotechnology, biology, and medicine · 2019Review
- Stimulation of Nipah Fusion: Small Intradomain Changes Trigger Extensive Interdomain Rearrangements.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a preliminary to the localization of the receptor-binding site(s) on the Nipah virus (NiV) glycoprotein (NiV-G), we have undertaken the identification of NiV-G residues that play a role in fusion promotion. To achieve this, we have used two strategies. First, as NiV and Hendra virus (HeV) share a common receptor and their cellular tropism is similar, we hypothesized that residues functioning in receptor attachment could be conserved between their respective G proteins. Our initial strategy was to target charged residues (which can be expected to be at the surface of the protein) conserved between the NiV-G and HeV-G globular heads. Second, we generated NiV variants that escaped neutralization by anti-NiV-G monoclonal antibodies (MAbs) that neutralize NiV both in vitro and in vivo, likely by blocking receptor attachment. The sequencing of such "escape mutants" identified NiV-G residues present in the epitopes to which the neutralizing MAbs are directed. Residues identified via these two strategies whose mutation had an effect on fusion promotion were localized on a new structural model for the NiV-G protein. Our results suggest that seven NiV-G residues, including one (E533) that was identified using both strategies, form a contiguous site on the top of the globular head that is implicated in ephrinB2 binding. This site commences near the shallow depression in the center of the top surface of the globular head and extends to the rim of the barrel-like structure on the top loops of beta-sheet 5. The topology of this site is strikingly similar to that proposed to form the SLAM receptor site on another paramyxovirus attachment protein, that of the measles virus hemagglutinin.
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