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

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.
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Article dans une revue
Nature Communications, Nature Publishing Group, 2013, 4, pp.1429
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http://hal.univ-grenoble-alpes.fr/hal-01101647
Contributeur : Frank Thomas <>
Soumis le : vendredi 9 janvier 2015 - 11:08:45
Dernière modification le : mardi 21 août 2018 - 14:12:01

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  • HAL Id : hal-01101647, version 1
  • PUBMED : 23385574

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Ambroise Desfosses, Euripedes A Ribeiro, Guy Schoehn, Danielle Blondel, Delphine Guilligay, et al.. Self-organization of the vesicular stomatitis virus nucleocapsid into a bullet shape.. Nature Communications, Nature Publishing Group, 2013, 4, pp.1429. 〈hal-01101647〉

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