Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex.
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ABSTRACT:
SUBMITTER: Kirchdoerfer RN
PROVIDER: S-EPMC4500542 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Publications
Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 Complex.
Kirchdoerfer Robert N RN Abelson Dafna M DM Li Sheng S Wood Malcolm R MR Saphire Erica Ollmann EO
Cell reports 20150625 1
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 conformation ...[more]
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