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Structural and biochemical characterization of nsp12-nsp7-nsp8 core polymerase complex from COVID-19 virus

By Qi Peng, Ruchao Peng, Bin Yuan, Jingru Zhao, Min Wang, Xixi Wang, Qian Wang, Yan Sun, Zheng Fan, Jianxun Qi, George F. Gao, Yi Shi

Posted 23 Apr 2020
bioRxiv DOI: 10.1101/2020.04.23.057265 (published DOI: 10.1016/j.celrep.2020.107774)

The ongoing global pandemic of coronavirus disease 2019 (COVID-19) has caused huge number of human deaths. Currently, there are no specific drugs or vaccines available for this virus. The viral polymerase is a promising antiviral target. However, the structure of COVID-19 virus polymerase is yet unknown. Here, we describe the near-atomic resolution structure of its core polymerase complex, consisting of nsp12 catalytic subunit and nsp7-nsp8 cofactors. This structure highly resembles the counterpart of SARS-CoV with conserved motifs for all viral RNA-dependent RNA polymerases, and suggests the mechanism for activation by cofactors. Biochemical studies revealed reduced activity of the core polymerase complex and lower thermostability of individual subunits of COVID-19 virus as compared to that of SARS-CoV. These findings provide important insights into RNA synthesis by coronavirus polymerase and indicate a well adaptation of COVID-19 virus towards humans with relatively lower body temperatures than the natural bat hosts. ### Competing Interest Statement The authors have declared no competing interest.

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