8UST

In-virion structure of Ebola virus nucleocapsid-like assemblies from recombinant virus-like particles (nucleoprotein, VP24,VP35,VP40)

Summary for 8UST

• Entry DOI: 10.2210/pdb8ust/pdb
• EMDB information: 3871
• Descriptor: Nucleoprotein, RNA (5'-R(*AP*AP*AP*AP*AP*A)-3'), Membrane-associated protein VP24, ... (4 entities in total)
• Functional Keywords: viral protein, nucleoprotein, nucleocapsid, ebola virus, ebov, filovirus, subtomogram averaging, in situ, viral protein-rna complex, viral protein/rna
• Biological source: Ebola virus - Mayinga, Zaire, 1976; More
• Total number of polymer chains: 9
• Total formula weight: 385331.23

Authors

Watanabe, R.,Zyla, D.,Saphire, E.O. (deposition date: 2023-10-29, release date: 2024-10-02, Last modification date: 2024-10-16)

Primary citation

Watanabe, R.,Zyla, D.,Parekh, D.,Hong, C.,Jones, Y.,Schendel, S.L.,Wan, W.,Castillon, G.,Saphire, E.O.
Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.
Cell, 187:5587-5603.e19, 2024

PubMed Abstract: Filoviruses, including the Ebola and Marburg viruses, cause hemorrhagic fevers with up to 90% lethality. The viral nucleocapsid is assembled by polymerization of the nucleoprotein (NP) along the viral genome, together with the viral proteins VP24 and VP35. We employed cryo-electron tomography of cells transfected with viral proteins and infected with model Ebola virus to illuminate assembly intermediates, as well as a 9 Å map of the complete intracellular assembly. This structure reveals a previously unresolved third and outer layer of NP complexed with VP35. The intrinsically disordered region, together with the C-terminal domain of this outer layer of NP, provides the constant width between intracellular nucleocapsid bundles and likely functions as a flexible tether to the viral matrix protein in the virion. A comparison of intracellular nucleocapsids with prior in-virion nucleocapsid structures reveals that the nucleocapsid further condenses vertically in the virion. The interfaces responsible for nucleocapsid assembly are highly conserved and offer targets for broadly effective antivirals.

PubMed: 39293445
DOI: 10.1016/j.cell.2024.08.044

Experimental method

ELECTRON MICROSCOPY (7.3 Å)