Self-organization of the vesicular stomatitis virus nucleocapsid into a bullet shape

Ambroise Desfosses, Euripedes A. Ribeiro, Guy Schoehn, Danielle Blondel, Delphine Guilligay, Marc Jamin, Rob W. H. Ruigrok and Irina Gutsche ()
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Ambroise Desfosses: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Euripedes A. Ribeiro: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Guy Schoehn: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Danielle Blondel: CNRS UPR 3296, Virologie Moléculaire et Structurale
Delphine Guilligay: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Marc Jamin: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Rob W. H. Ruigrok: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions
Irina Gutsche: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions

Nature Communications, 2013, vol. 4, issue 1, 1-5

Abstract: Abstract The typical bullet shape of Rhabdoviruses is thought to rely on the matrix protein for stabilizing the nucleocapsid coil. Here we scrutinize the morphology of purified and recombinant nucleocapsids of vesicular stomatitis virus in vitro. We elucidate pH and ionic strength conditions for their folding into conical tips and further growth into whole bullets, and provide cryo-electron microscopy reconstructions of the bullet tip and the helical trunk. We address conformational variability of the reconstituted nucleocapsids and the issue of constraints imposed by the binding of matrix protein. Our findings bridge the gap between the isolated nucleoprotein-RNA string in its form of an undulating ribbon, and the tight bullet-shaped virion skeleton.

Date: 2013
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DOI: 10.1038/ncomms2435

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