ArticlePloS one2010
Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 83 citations in OpenAlex.
- Sequence-encoded determinants drive distinct early aggregation pathways and different structural outcomes in PNT1 fibrils across Henipavirus members.Protein science : a publication of the Protein Society · 2026Article
- Hendra virus genotypes 1 and 2 differ in V protein-mediated immune evasion.The Journal of general virology · 2026Article
- Respiratory syncytial virus phosphoprotein has NTPase and helicase-like activities.Journal of virology · 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
- 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
- Dissecting Henipavirus W proteins conformational and fibrillation properties: contribution of their N- and C-terminal constituent domains.The FEBS journal · 2025Article
- Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation.The journal of physical chemistry letters · 2024Article
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- Article
- Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies.International journal of molecular sciences · 2022Article
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins.Biomolecules · 2022Article
- Experimental Evidence of Intrinsic Disorder and Amyloid Formation by theInternational journal of molecular sciences · 2022Article
- Predicting Protein Conformational Disorder and Disordered Binding Sites.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
- Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation.Biomolecules · 2021Article
- CryoEM structure of the Nipah virus nucleocapsid assembly.PLoS pathogens · 2021Article
- Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy.Nature nanotechnology · 2021Article
- Predicting substitutions to modulate disorder and stability in coiled-coils.BMC bioinformatics · 2020Article
- Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.Scientific reports · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Henipaviruses are newly emerged viruses within the Paramyxoviridae family. Their negative-strand RNA genome is packaged by the nucleoprotein (N) within alpha-helical nucleocapsid that recruits the polymerase complex made of the L protein and the phosphoprotein (P). To date structural data on Henipaviruses are scarce, and their N and P proteins have never been characterized so far. Using both computational and experimental approaches we herein show that Henipaviruses N and P proteins possess large intrinsically disordered regions. By combining several disorder prediction methods, we show that the N-terminal domain of P (PNT) and the C-terminal domain of N (NTAIL) are both mostly disordered, although they contain short order-prone segments. We then report the cloning, the bacterial expression, purification and characterization of Henipavirus PNT and NTAIL domains. By combining gel filtration, dynamic light scattering, circular dichroism and nuclear magnetic resonance, we show that both NTAIL and PNT belong to the premolten globule sub-family within the class of intrinsically disordered proteins. This study is the first reported experimental characterization of Henipavirus P and N proteins. The evidence that their respective N-terminal and C-terminal domains are highly disordered under native conditions is expected to be invaluable for future structural studies by helping to delineate N and P protein domains amenable to crystallization. In addition, following previous hints establishing a relationship between structural disorder and protein interactivity, the present results suggest that Henipavirus PNT and NTAIL domains could be involved in manifold protein-protein interactions.
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