Structure Basis for Inhibition of SARS-CoV-2 by the Feline Drug GC376
Xiaodong Luan, Weijuan Shang, Yifei Wang, Wanchao Yin, Yi Jiang, Siqin Feng, Yiyang Wang, Meixi Liu, Ruilin Zhou, Zhiyu Zhang, Feng Wang, Wang Cheng, Minqi Gao, Hui Wang, Wei Wu, Ran Tian, Zhuang Tian, Ye Jin, Hualiang Jiang, Leike Zhang, H. Eric Xu, Shuyang Zhang
Abstract
The pandemic of SARS-CoV-2 coronavirus disease-2019 (COVID-19) caused by SARS-COV-2 continues to ravage many countries in the world. Mpro is an indispensable protein for viral translation in SARS-CoV-2 and a potential target in high-specificity anti-SARS-CoV-2 drug screening. In this study, to explore potential drugs for treating COVID-19, we elucidated the structure of SARS-CoV-2 Mpro and explored the interaction between Mpro and GC376, an antiviral drug used to treat a range of coronaviruses in Feline via inhibiting Mpro. The availability and safety of GC376 were proved by biochemical and cell experiments in vitro. We determined the structure of an important protein, Mpro, in SARS-CoV-2, and revealed the interaction of GC376 with the viral substrate and inhibition of the catalytic site of SARS-CoV-2 Mpro.
CORDITE (CORona Drug InTEractions database) collects and aggregates data from PubMed, MedRxiv, BioRxiv, ChemRxiv and PMC for SARS-CoV-2. Its main focus is set on drug interactions either addressing viral proteins or human proteins that could be used to treat COVID.
It collects and provides up-to-date information on computational predictions, in vitro, as well as in vivo study data.
The information provided is for research only and we cannot guarantee the correctness of the data.
