Structural highlights
Publication Abstract from PubMedEbola 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 A using electron cryo-microscopy and identified a new regulatory role for eNP helices alpha22-alpha23. Biochemical, biophysical, and mutational analyses revealed that inter-eNP contacts within alpha22-alpha23 are critical for viral NC assembly and regulate viral RNA synthesis. These observations suggest that the N terminus and alpha22-alpha23 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. Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.,Su Z, Wu C, Shi L, Luthra P, Pintilie GD, Johnson B, Porter JR, Ge P, Chen M, Liu G, Frederick TE, Binning JM, Bowman GR, Zhou ZH, Basler CF, Gross ML, Leung DW, Chiu W, Amarasinghe GK Cell. 2018 Feb 22;172(5):966-978.e12. doi: 10.1016/j.cell.2018.02.009. PMID:29474922[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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