8USN
Intracellular cryo-tomography structure of EBOV nucleocapsid at 8.9 Angstrom
Summary for 8USN
Entry DOI | 10.2210/pdb8usn/pdb |
EMDB information | 42509 |
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, cryo-et, fib, intracellular, in situ |
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: 2023-10-27, release date: 2024-10-02, Last modification date: 2024-11-13) |
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 Cited by 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: 39293445DOI: 10.1016/j.cell.2024.08.044 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.9 Å) |
Structure validation
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