6EHL

Model of the Ebola virus nucleoprotein in recombinant nucleocapsid-like assemblies

Summary for 6EHL

• Entry DOI: 10.2210/pdb6ehl/pdb
• EMDB information: 3869
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: nucleocapsid, virus like particle
• Biological source: Zaire ebolavirus (strain Mayinga-76) (ZEBOV)
• Total number of polymer chains: 1
• Total formula weight: 83387.50

Authors

Wan, W.,Kolesnikova, L.,Clarke, M.,Koehler, A.,Noda, T.,Becker, S.,Briggs, J.A.G. (deposition date: 2017-09-13, release date: 2017-11-08, Last modification date: 2024-05-22)

Primary citation

Wan, W.,Kolesnikova, L.,Clarke, M.,Koehler, A.,Noda, T.,Becker, S.,Briggs, J.A.G.
Structure and assembly of the Ebola virus nucleocapsid.
Nature, 551:394-397, 2017

PubMed 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.

PubMed: 29144446
DOI: 10.1038/nature24490

Experimental method

ELECTRON MICROSCOPY (6.6 Å)