ArticleStructure (London, England : 1993)2019
A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for Polymerase Function.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Assessing the pandemic potential of Nipah virus: From molecular pathogenesis to ecological spillover risks.Infectious medicine · 2026Review
- The Silent Spillover Threat: Nipah Virus Epidemiology, Pathogenesis, Clinical Manifestations, and Advances in Therapeutics and Vaccine Development.Microorganisms · 2026Review
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Construction of Minigenome Replicon of Nipah Virus and Investigation of Biological Activity.Viruses · 2025Article
- Henipaviruses: epidemiology, ecology, disease, and the development of vaccines and therapeutics.Clinical microbiology reviews · 2025Review
- Structure of the Nipah virus polymerase phosphoprotein complex.Nature communications · 2024Article
- A Comparative Assessment of the Pathogenic Potential of Newly Discovered Henipaviruses.Pathogens (Basel, Switzerland) · 2024Review
- Indiscriminate activities of different henipavirus polymerase complex proteins allow for efficient minigenome replication in hybrid systems.Journal of virology · 2024Article
- Structures of the mumps virus polymerase complex via cryo-electron microscopy.Nature communications · 2024Article
- Genomic characterization, transcriptome analysis, and pathogenicity of the Nipah virus (Indian isolate).Virulence · 2023Article
- Single-dose mucosal replicon-particle vaccine protects against lethal Nipah virus infection up to 3 days after vaccination.Science advances · 2023Article
- GCRV NS38 counteracts SVCV proliferation by intracellular antagonization during co-infection.Virologica Sinica · 2023Article
- Article
- Evolutionary history of cotranscriptional editing in the paramyxoviral phosphoprotein gene.Virus evolution · 2021Review
- Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus.Journal of virology · 2020Article
- Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1.Biophysical journal · 2020Article
- Vesicular Stomatitis Virus Phosphoprotein Dimerization Domain Is Dispensable for Virus Growth.Journal of virology · 2020Article
- Bipartite interface of the measles virus phosphoprotein X domain with the large polymerase protein regulates viral polymerase dynamics.PLoS pathogens · 2019Article
- The Nucleoprotein and Phosphoprotein of Measles Virus.Frontiers in microbiology · 2019Review
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Authors and funding
5 authors.
Funding
Abstract
Nipah virus is a highly lethal zoonotic pathogen found in Southeast Asia that has caused human encephalitis outbreaks with 40%-70% mortality. NiV encodes its own RNA-dependent RNA polymerase within the large protein, L. Efficient polymerase activity requires the phosphoprotein, P, which tethers L to its template, the viral nucleocapsid. P is a multifunctional protein with modular domains. The central P multimerization domain is composed of a long, tetrameric coiled coil. We investigated the importance of structural features found in this domain for polymerase function using a newly constructed NiV bicistronic minigenome assay. We identified a conserved basic patch and central kink in the coiled coil that are important for polymerase function, with R555 being absolutely essential. This basic patch and central kink are conserved in the related human pathogens measles and mumps viruses, suggesting that this mechanism may be conserved.
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