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8Y9J

Structure of the Ebola virus nucleocapsid subunit

Summary for 8Y9J
Entry DOI10.2210/pdb8y9j/pdb
EMDB information39081
DescriptorNucleoprotein, Membrane-associated protein VP24, RNA (12-MER) (3 entities in total)
Functional Keywordscomplex, viral protein, viral protein-rna complex, viral protein/rna
Biological sourceZaire ebolavirus
More
Total number of polymer chains5
Total formula weight226905.65
Authors
Fujita-Fujiharu, Y.,Hu, S.,Hirabayashi, A.,Takamatsu, Y.,Ng, Y.,Houri, K.,Muramoto, Y.,Nakano, M.,Sugita, Y.,Noda, T. (deposition date: 2024-02-06, release date: 2025-01-29, Last modification date: 2025-07-02)
Primary citationFujita-Fujiharu, Y.,Hu, S.,Hirabayashi, A.,Takamatsu, Y.,Ng, Y.N.,Houri, K.,Muramoto, Y.,Nakano, M.,Sugita, Y.,Noda, T.
Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24.
Nat Commun, 16:2171-2171, 2025
Cited by
PubMed Abstract: The Ebola virus, a member of the Filoviridae family, causes severe hemorrhagic fever in humans. Filamentous virions contain a helical nucleocapsid responsible for genome transcription, replication, and packaging into progeny virions. The nucleocapsid consists of a helical nucleoprotein (NP)-viral genomic RNA complex forming the core structure, to which VP24 and VP35 bind externally. Two NPs, each paired with a VP24 molecule, constitute a repeating unit. However, the detailed nucleocapsid structure remains unclear. Here, we determine the nucleocapsid-like structure within virus-like particles at 4.6 Å resolution using single-particle cryo-electron microscopy. Mutational analysis identifies specific interactions between the two NPs and two VP24s and demonstrates that each of the two VP24s in different orientations distinctively regulates nucleocapsid assembly, viral RNA synthesis, intracellular transport of the nucleocapsid, and infectious virion production. Our findings highlight the sophisticated mechanisms underlying the assembly and functional regulation of the nucleocapsid and provide insights into antiviral development.
PubMed: 40064872
DOI: 10.1038/s41467-025-57236-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.6 Å)
Structure validation

239492

数据于2025-07-30公开中

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