Structure of the Vesicular Stomatitis Virus N0-P Complex
Author Information
Author(s): Cédric Leyrat, Filip Yabukarski, Nicolas Tarbouriech, Euripedes A. Ribeiro Jr., Malene Ringkjøbing Jensen, Martin Blackledge, Rob W. H. Ruigrok, Marc Jamin
Primary Institution: UMI 3265 UJF-EMBL-CNRS Unit of Virus Host Cell Interactions, Grenoble, France
Hypothesis
How does the N0-P complex of vesicular stomatitis virus facilitate viral RNA synthesis?
Conclusion
The study reveals the structural details of the N0-P complex, showing how it prevents RNA binding and self-assembly of nucleoprotein N.
Supporting Evidence
- The N0-P complex prevents the nucleoprotein from binding to cellular RNAs.
- The structure of the N0-P complex was solved at 3.0 Å resolution.
- NMR spectroscopy confirmed the binding of the MoRE of P to N.
- The complex crystallized in a decameric circular form.
- Binding of the MoRE modifies the electrostatic surface potential of N.
Takeaway
The N0-P complex helps the virus make copies of its RNA by keeping the nucleoprotein in a form that doesn't stick to other things it shouldn't.
Methodology
The complex was characterized using X-ray crystallography, NMR spectroscopy, and small-angle X-ray scattering.
Limitations
The study primarily focuses on a specific complex and may not represent all forms of the nucleoprotein.
Digital Object Identifier (DOI)
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