RT Journal Article
SR Electronic
T1 Structural and biochemical characterization of nsp12-nsp7-nsp8 core polymerase complex from COVID-19 virus
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.04.23.057265
DO 10.1101/2020.04.23.057265
A1 Qi Peng
A1 Ruchao Peng
A1 Bin Yuan
A1 Jingru Zhao
A1 Min Wang
A1 Xixi Wang
A1 Qian Wang
A1 Yan Sun
A1 Zheng Fan
A1 Jianxun Qi
A1 George F. Gao
A1 Yi Shi
YR 2020
UL http://biorxiv.org/content/early/2020/04/23/2020.04.23.057265.abstract
AB 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 StatementThe authors have declared no competing interest.