title: 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.
authors: UJF-EMBL-CNRS UMI 3265, Unit of Virus Host Cell Interactions, Grenoble, France.
authors: Ambroise
authors: A
authors: Desfosses
authors: Euripedes A
authors: EA
authors: Ribeiro
authors: Guy
authors: G
authors: Schoehn
authors: Danielle
authors: D
authors: Blondel
authors: Delphine
authors: D
authors: Guilligay
authors: Marc
authors: M
authors: Jamin
authors: Rob W H
authors: RW
authors: Ruigrok
authors: Irina
authors: I
authors: Gutsche
mesh_terms: D020285:Cryoelectron Microscopy; D009690:Nucleic Acid Conformation; D019251:Nucleocapsid / Q000648:ultrastructure*; D009698:Nucleoproteins / Q000378:metabolism; D012367:RNA, Viral / Q000648:ultrastructure; D014721:Vesicular stomatitis Indiana virus / Q000648:ultrastructure*; D014763:Viral Matrix Proteins / Q000378:metabolism
chemical_list: D009698:Nucleoproteins; D012367:RNA, Viral; D014763:Viral Matrix Proteins
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