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Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex

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Journal Cell Rep
Publisher Cell Press
Date 2015 Jun 30
PMID 26119732
Citations 80
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Abstract

Ebolavirus NP oligomerizes into helical filaments found at the core of the virion, encapsidates the viral RNA genome, and serves as a scaffold for additional viral proteins within the viral nucleocapsid. We identified a portion of the phosphoprotein homolog VP35 that binds with high affinity to nascent NP and regulates NP assembly and viral genome binding. Removal of the VP35 peptide leads to NP self-assembly via its N-terminal oligomerization arm. NP oligomerization likely causes a conformational change between the NP N- and C-terminal domains, facilitating RNA binding. These functional data are complemented by crystal structures of the NP°-VP35 complex at 2.4 Å resolution. The interactions between NP and VP35 illuminated by these structures are conserved among filoviruses and provide key targets for therapeutic intervention.

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References
1.
ELLIOTT L, Kiley M, McCormick J . Descriptive analysis of Ebola virus proteins. Virology. 1985; 147(1):169-76. DOI: 10.1016/0042-6822(85)90236-3. View

2.
Majumdar A, Bhattacharya R, Basak S, Shaila M, Chattopadhyay D, Roy S . P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage. Biochemistry. 2004; 43(10):2863-70. DOI: 10.1021/bi035793r. View

3.
Watanabe S, Noda T, Kawaoka Y . Functional mapping of the nucleoprotein of Ebola virus. J Virol. 2006; 80(8):3743-51. PMC: 1440433. DOI: 10.1128/JVI.80.8.3743-3751.2006. View

4.
Tawar R, Duquerroy S, Vonrhein C, Varela P, Damier-Piolle L, Castagne N . Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus. Science. 2009; 326(5957):1279-83. DOI: 10.1126/science.1177634. View

5.
Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro Jr E, Jensen M, Blackledge M . Structure of the vesicular stomatitis virus N⁰-P complex. PLoS Pathog. 2011; 7(9):e1002248. PMC: 3178552. DOI: 10.1371/journal.ppat.1002248. View