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Structure and assembly of the Ebola virus nucleocapsid.

Structure and assembly of the Ebola virus nucleocapsid.
Author Information (click to view)

Wan W, Kolesnikova L, Clarke M, Koehler A, Noda T, Becker S, Briggs JAG,


Wan W, Kolesnikova L, Clarke M, Koehler A, Noda T, Becker S, Briggs JAG, (click to view)

Wan W, Kolesnikova L, Clarke M, Koehler A, Noda T, Becker S, Briggs JAG,

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Nature 2017 11 08551(7680) 394-397 doi 10.1038/nature24490
Abstract

Ebola and Marburg viruses are filoviruses: filamentous, enveloped viruses that cause haemorrhagic fever. Filoviruses are within the order Mononegavirales, which also includes rabies virus, measles virus, and respiratory syncytial virus. Mononegaviruses have non-segmented, single-stranded negative-sense RNA genomes that are encapsidated by nucleoprotein and other viral proteins to form a helical nucleocapsid. The nucleocapsid acts as a scaffold for virus assembly and as a template for genome transcription and replication. Insights into nucleoprotein-nucleoprotein interactions have been derived from structural studies of oligomerized, RNA-encapsidating nucleoprotein, and cryo-electron microscopy of nucleocapsid or nucleocapsid-like structures. There have been no high-resolution reconstructions of complete mononegavirus nucleocapsids. Here we apply cryo-electron tomography and subtomogram averaging to determine the structure of Ebola virus nucleocapsid within intact viruses and recombinant nucleocapsid-like assemblies. These structures reveal the identity and arrangement of the nucleocapsid components, and suggest that the formation of an extended α-helix from the disordered carboxy-terminal region of nucleoprotein-core links nucleoprotein oligomerization, nucleocapsid condensation, RNA encapsidation, and accessory protein recruitment.

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