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Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
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Toscana virus nucleoprotein oligomer organization observed in solution
Amal Baklouti1, Adeline Goulet1, Julie Lichière1
1Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 13288 Marseille, France.
Acta Crystallographica. Section D, Structural Biology
|August 5, 2017
Summary
Toscana virus nucleoprotein (N) forms open oligomers in solution, reconciling structural data with observed ribonucleoprotein complex organization. This finding clarifies the RNA encapsidation mechanism in phleboviruses.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Toscana virus (TOSV) is an arthropod-borne phlebovirus with a three-segment RNA genome.
- The nucleoprotein (N) encapsidates the viral RNA and is crucial for replication.
- Existing crystallographic data show closed-ring N structures, contrasting with electron microscopy of filamentous ribonucleoprotein (RNP) complexes.
Purpose of the Study:
- To investigate the structural organization of recombinant TOSV N.
- To reconcile discrepancies between crystallographic N structures and RNP complex morphology.
- To elucidate the phlebovirus RNA encapsidation mechanism.
Main Methods:
- Integrative structural biology approach.
- X-ray diffraction crystallography.
- Transmission electron microscopy (TEM).
- Small-angle X-ray scattering (SAXS).
- Size-exclusion chromatography (SEC).
- Multi-angle laser light scattering (MALLS).
Main Results:
- TOSV N forms open oligomers in solution.
- These oligomeric states are consistent with the observed filamentous RNP structure.
- The findings bridge the gap between atomic resolution crystal structures and lower-resolution complex visualizations.
Conclusions:
- The study reveals a dynamic, oligomeric state of TOSV N in solution.
- This structure supports a model for phlebovirus RNA encapsidation.
- The findings advance understanding of bunyavirus RNP assembly and structure.
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