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Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04

Cell Discov . 2024-04; 
Lijing Zhang, Xuping Xie, Hannan Luo, Runtong Qian, Yang Yang, Hongtao Yu, Jing Huang, Pei-Yong Shi, Qi Hu
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Proteins, Expression, Isolation and Analysis In brief, the His-tagged proteins were purified by affinity chromatography using Co2+ resin (TALON, 635504), then the tag was removed by human rhinovirus 3C protease (TaKaRa, 7360) and the efficiency of cleavage was analyzed by SDS-PAGE (GenScript,M00656) Get A Quote

摘要

Drug resistance poses a significant challenge in the development of effective therapies against SARS-CoV-2. Here, we identified two double mutations, M49K/M165V and M49K/S301P, in the 3C-like protease (3CLpro) that confer resistance to a novel non-covalent inhibitor, WU-04, which is currently in phase III clinical trials (NCT06197217). Crystallographic analysis indicates that the M49K mutation destabilizes the WU-04-binding pocket, impacting the binding of WU-04 more significantly than the binding of 3CLpro substrates. The M165V mutation directly interferes with WU-04 binding. The S301P mutation, which is far from the WU-04-binding pocket, indirectly affects WU-04 binding by restricting the rotation of 3CLpro's... More

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