ArticleNature communications2024
Cryo-EM structure of Nipah virus L-P polymerase 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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Nipah virus in the era of global connectivity: molecular evolution, transmission risk, and preparedness strategies.Virus genes · 2026Review
- Nipah Virus: A Neurotropic Zoonosis-From Molecular Biology to Clinical Manifestations and Translational Advances.Viruses · 2026Review
- Machine learning-driven drug repurposing and computational validation for Nipah virus.Molecular diversity · 2026Article
- Unreacted RSV Polymerase Structures Expand the Post-Translocation Landscape of the Nucleotide Addition Cycle.Microorganisms · 2026Article
- mRNA cap formation by the human respiratory syncytial virus large protein.Nucleic acids research · 2026Article
- Targeting the RSV and hMPV L Protein: Cryo-EM and Structure-Based Approaches to Antiviral Drug Discovery.Biomolecules · 2026Review
- Structural basis for RNA synthesis and inhibition of the orthobunyavirus polymerase.Nature communications · 2026Article
- 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
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- 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
- Construction of Minigenome Replicon of Nipah Virus and Investigation of Biological Activity.Viruses · 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
- Structural basis of Nipah virus RNA synthesis.Nature communications · 2025Article
- Review
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Authors and funding
7 authors.
Funding
Abstract
Nipah virus (NiV) is a non-segmented, negative-strand (NNS) RNA virus, belonging to Paramyxoviridae. The RNA polymerase complex, composed of large (L) protein and tetrameric phosphoprotein (P), is responsible for genome transcription and replication by catalyzing NTP polymerization, mRNA capping and cap methylation. Here, we determine the cryo-electron microscopy (cryo-EM) structure of fully bioactive NiV L-P polymerase complex at a resolution of 3.19 Å. The L-P complex displays a conserved architecture like other NNS RNA virus polymerases and L interacts with the oligomerization domain and the extreme C-terminus region of P tetramer. Moreover, we elucidate that NiV is naturally resistant to the allosteric L-targeting inhibitor GHP-88309 due to the conformational change in the drug binding site. We also find that the non-nucleotide drug suramin can inhibit the NiV L-P polymerase activity at both the enzymatic and cellular levels. Our findings have greatly enhanced the molecular understanding of NiV genome replication and transcription and provided the rationale for broad-spectrum polymerase-targeted drug design.
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