Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.

ABSTRACT: Ebola virus nucleoprotein (eNP) assembles into higher-ordered structures that form the viral nucleocapsid (NC) and serve as the scaffold for viral RNA synthesis. However, molecular insights into the NC assembly process are lacking. Using a hybrid approach, we characterized the NC-like assembly of eNP, identified novel regulatory elements, and described how these elements impact function. We generated a three-dimensional structure of the eNP NC-like assembly at 5.8 Å using electron cryo-microscopy and identified a new regulatory role for eNP helices ?22-?23. Biochemical, biophysical, and mutational analyses revealed that inter-eNP contacts within ?22-?23 are critical for viral NC assembly and regulate viral RNA synthesis. These observations suggest that the N terminus and ?22-?23 of eNP function as context-dependent regulatory modules (CDRMs). Our current study provides a framework for a structural mechanism for NC-like assembly and a new therapeutic target.

SUBMITTER: Su Z 

PROVIDER: S-EPMC5973842 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature