Structural and biochemical characterization of nsp12-nsp7-nsp8 core polymerase complex from COVID-19 virus
George F. Gao,
Posted 23 Apr 2020
bioRxiv DOI: 10.1101/2020.04.23.057265 (published DOI: 10.1016/j.celrep.2020.107774)
Posted 23 Apr 2020
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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