Publication Date

6-28-2022

Journal

mBio

DOI

10.1128/mbio.00784-22

PMID

35471084

PMCID

PMC9239272

PubMedCentral® Posted Date

4-26-2022

PubMedCentral® Full Text Version

Post-print

Published Open-Access

yes

Keywords

Amino Acids, Antiviral Agents, Coronavirus 3C Proteases, Luciferases, Firefly, Protease Inhibitors, SARS-CoV-2/, coronavirus, gain-of-signal cell-based systems, main protease (Mpro/3CLpro), SARS-CoV-2 (SARS2), viral protease inhibitors

Abstract

The main protease, Mpro, of SARS-CoV-2 is required to cleave the viral polyprotein into precise functional units for virus replication and pathogenesis. Here, we report quantitative reporters for Mpro function in living cells in which protease inhibition by genetic or chemical methods results in robust signal readouts by fluorescence (enhanced green fluorescent protein [eGFP]) or bioluminescence (firefly luciferase). These gain-of-signal systems are scalable to high-throughput platforms for quantitative discrimination between Mpro mutants and/or inhibitor potencies as evidenced by validation of several reported inhibitors. Additional utility is shown by single Mpro amino acid variants and structural information combining to demonstrate that both inhibitor conformational dynamics and amino acid differences are able to influence inhibitor potency. We further show that a recent variant of concern (Omicron) has an unchanged response to a clinically approved drug, nirmatrelvir, whereas proteases from divergent coronavirus species show differential susceptibility. Together, we demonstrate that these gain-of-signal systems serve as robust, facile, and scalable assays for live cell quantification of Mpro inhibition, which will help expedite the development of next-generation antivirals and enable the rapid testing of emerging variants.

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