ArticleNature communications2024
Structure of the Nipah virus polymerase phosphoprotein complex.
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 20 papers.
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Who cites it
20 citing papers in PubMed.
- Machine learning-driven drug repurposing and computational validation for Nipah virus.Molecular diversity · 2026Article
- Proteome conserved multi-epitope-based vaccine construct against Nipah virus.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Unreacted RSV Polymerase Structures Expand the Post-Translocation Landscape of the Nucleotide Addition Cycle.Microorganisms · 2026Article
- Epitope-based vaccine of NiV targeting glycoprotein and fusion protein: an integrated immunoinformatics and bioinformatics approach.Virus research · 2026Article
- Structural insights into the Nipah virus nucleocapsid assembly.Communications biology · 2026Article
- The Silent Spillover Threat: Nipah Virus Epidemiology, Pathogenesis, Clinical Manifestations, and Advances in Therapeutics and Vaccine Development.Microorganisms · 2026Review
- Small Molecule Inhibition of Mononegavirales RNA Polymerases.Journal of medical virology · 2026Review
- Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.Nature communications · 2026Article
- Efficacy of the nucleoside analog 4'-Fluorouridine against Nipah virus in the Syrian hamster model.PLoS pathogens · 2026Article
- Engineering Nipah virus: Reverse genetics as a gateway to novel drug discovery.New microbes and new infections · 2026Review
- Structural basis of measles virus polymerase inhibition by nonnucleoside inhibitor ERDRP-0519.Nature communications · 2025Article
- Structural insights into the dynamic mechanism of bornavirus polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery.Nature communications · 2025Article
- Immunoinformatics-driven design of a multi-epitope vaccine against nipah virus: A promising approach for global health protection.Journal, genetic engineering & biotechnology · 2025Article
- A deep learning and molecular modeling approach to repurposing Cangrelor as a potential inhibitor of Nipah virus.Scientific reports · 2025Article
- Structure of the measles virus ternary polymerase complex.Nature communications · 2025Article
- Functional dissection of the C-terminal domain of rabies virus RNA polymerase L protein.Journal of virology · 2025Article
- Structural basis of Nipah virus RNA synthesis.Nature communications · 2025Article
- Uncovering human kinase substrates in nipah proteome.Frontiers in bioinformatics · 2025Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Nipah virus (NiV), a member of the Paramyxoviridae family, is notorious for its high fatality rate in humans. The RNA polymerase machinery of NiV, comprising the large protein L and the phosphoprotein P, is essential for viral replication. This study presents the 2.9-Å cryo-electron microscopy structure of the NiV L-P complex, shedding light on its assembly and functionality. The structure not only demonstrates the molecular details of the conserved N-terminal domain, RNA-dependent RNA polymerase (RdRp), and GDP polyribonucleotidyltransferase of the L protein, but also the intact central oligomerization domain and the C-terminal X domain of the P protein. The P protein interacts extensively with the L protein, forming an antiparallel β-sheet among the P protomers and with the fingers subdomain of RdRp. The flexible linker domain of one P promoter extends its contact with the fingers subdomain to reach near the nascent RNA exit, highlighting the distinct characteristic of the NiV L-P interface. This distinctive tetrameric organization of the P protein and its interaction with the L protein provide crucial molecular insights into the replication and transcription mechanisms of NiV polymerase, ultimately contributing to the development of effective treatments and preventive measures against this Paramyxoviridae family deadly pathogen.
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