ArticleBiophysical journal2020
Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1.
Article in Biophysical journal, 2020. 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, 54 citations in OpenAlex.
- Development of a novel hybrid alphavirus-Nipah virus pseudovirion for rapid quantification of vaccine-induced neutralization antibodies.Emerging microbes & infections · 2026Article
- Mpox virus D8L protein binds to STAT1 and inhibits its phosphorylation to antagonize IFN-induced signaling.Cell communication and signaling : CCS · 2026Article
- Efficacy of the nucleoside analog 4'-Fluorouridine against Nipah virus in the Syrian hamster model.PLoS pathogens · 2026Article
- Consequences of Peptide Macrocyclization Revealed by Virus-Inspired β-Hairpin Mimetics.ACS chemical biology · 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
- Identification of conserved CD8+ T cell epitopes in Nipah virus towards vaccine development using an immunoinformatics approach.Clinical and experimental vaccine research · 2025Article
- A deep learning and molecular modeling approach to repurposing Cangrelor as a potential inhibitor of Nipah virus.Scientific reports · 2025Article
- A conserved motif in Henipavirus P/V/W proteins drives the fibrillation of the W protein from Hendra virus.Protein science : a publication of the Protein Society · 2025Article
- Henipaviruses: epidemiology, ecology, disease, and the development of vaccines and therapeutics.Clinical microbiology reviews · 2025Review
- Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unraveling the molecular grammar and the structural transitions underlying the fibrillation of a viral fibrillogenic domain.Protein science : a publication of the Protein Society · 2025Article
- Article
- Dissecting Henipavirus W proteins conformational and fibrillation properties: contribution of their N- and C-terminal constituent domains.The FEBS journal · 2025Article
- Nipah virus: epidemiology, pathogenesis, treatment, and prevention.Frontiers of medicine · 2024Review
- Dimerization of Rabies Virus Phosphoprotein and Phosphorylation of Its Nucleoprotein Enhance Their Binding Affinity.Viruses · 2024Article
- Evaluation of the interaction between potent small molecules against the Nipah virus Glycoprotein in Malaysia and Bangladesh strains, accompanied by the human Ephrin-B2 and Ephrin-B3 receptors; a simulation approach.Molecular diversity · 2024Article
- A comparative genomic approach to decipher the mutations associated with Nipah viral human isolates from southeast Asia.Iranian journal of microbiology · 2024Article
- Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023Review
- Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural characterization of modular proteins containing long intrinsically disordered regions intercalated with folded domains is complicated by their conformational diversity and flexibility and requires the integration of multiple experimental approaches. Nipah virus (NiV) phosphoprotein, an essential component of the viral RNA transcription/replication machine and a component of the viral arsenal that hijacks cellular components and counteracts host immune responses, is a prototypical model for such modular proteins. Curiously, the phosphoprotein of NiV is significantly longer than the corresponding protein of other paramyxoviruses. Here, we combine multiple biophysical methods, including x-ray crystallography, NMR spectroscopy, and small angle x-ray scattering, to characterize the structure of this protein and provide an atomistic representation of the full-length protein in the form of a conformational ensemble. We show that full-length NiV phosphoprotein is tetrameric, and we solve the crystal structure of its tetramerization domain. Using NMR spectroscopy and small angle x-ray scattering, we show that the long N-terminal intrinsically disordered region and the linker connecting the tetramerization domain to the C-terminal X domain exchange between multiple conformations while containing short regions of residual secondary structure. Some of these transient helices are known to interact with partners, whereas others represent putative binding sites for yet unidentified proteins. Finally, using NMR spectroscopy and isothermal titration calorimetry, we map a region of the phosphoprotein, comprising residues between 110 and 140 and common to the V and W proteins, that binds with weak affinity to STAT1 and confirm the involvement of key amino acids of the viral protein in this interaction. This provides new, to our knowledge, insights into how the phosphoprotein and the nonstructural V and W proteins of NiV perform their multiple functions.
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