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. 2018 Apr;28(4):497-499.
doi: 10.1038/s41422-018-0007-9. Epub 2018 Feb 21.

Structural insight into the Zika virus capsid encapsulating the viral genome

Ting Li  1   2 , Qi Zhao  3 , Xiaoyun Yang  1 , Cheng Chen  1 , Kailin Yang  4 , Chen Wu  1 , Tianqing Zhang  1 , Yinkai Duan  1 , Xiaoyu Xue  3 , Kaixia Mi  5 , Xiaoyun Ji  6 , Zefang Wang  1 , Haitao Yang  7   8
Affiliations

Structural insight into the Zika virus capsid encapsulating the viral genome

Ting Li et al. Cell Res. 2018 Apr.
No abstract available

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Conflict of interest statement

The authors declare no competing financial interests.

Figures

Fig. 1
Fig. 1
The overall structure of the ZIKV C protein shows a positively charged path on the dimeric ZIKV C protein surface that is essential for nucleic acid binding. a Ribbon diagram of the ZIKV C protein dimer colored with light blue (Protomer A) and light pink (Protomer B), respectively. b–d Close-up views of the dimer interface. Hydrophobic residues involved in dimerization include the N-terminal interface (b), the α2A–α2B interface (c), and the α4A–α4B interface (d). e EMSA assay of ZIKVCL binding to ssDNA in a dose-dependent manner. Lane 1: 100 ng free ssDNA; lanes 2–6: ZIKVCL protein of various concentrations was incubated with 100 ng free ssDNA. f EMSA assay of ZIKVCL mutants binding to ssDNA. Lane 1: 100 ng free ssDNA; lanes 2–3: WT ZIKVCL; lanes 4–5: M1; lanes 6–7: M2; lanes 8–9: M3; lane 10: MBP as a negative control. g A ribbon diagram labeled with positive residues on the surface of the ZIKV C protein dimer in different views and its corresponding electrostatic potential surface of the ZIKV C protein dimer. An uninterrupted positively charged path was identified as wrapping around the entire molecule
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