Nature communications · 2020
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication.
СтатьяПоддержка NIH: внешняя программаПоддержка исследования: вне правительства СШАПоддержка правительства СШАНазвание и аннотация: Перевод пока не подготовлен
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Vuong Wayne, Khan Muhammad Bashir, Fischer Conrad, Arutyunova Elena, Lamer Tess, Shields Justin, Saffran Holly A, McKay Ryan T, van Belkum Marco J, Joyce Michael A, Young Howard S, Tyrrell D Lorne, Vederas John C, Lemieux M Joanne
Аннотация
The main protease, Mpro (or 3CLpro) in SARS-CoV-2 is a viable drug target because of its essential role in the cleavage of the virus polypeptide. Feline infectious peritonitis, a fatal coronavirus infection in cats, was successfully treated previously with a prodrug GC376, a dipeptide-based protease inhibitor. Here, we show the prodrug and its parent GC373, are effective inhibitors of the Mpro from both SARS-CoV and SARS-CoV-2 with IC50 values in the nanomolar range. Crystal structures of SARS-CoV-2 Mpro with these inhibitors have a covalent modification of the nucleophilic Cys145. NMR analysis reveals that inhibition proceeds via reversible formation of a hemithioacetal. GC373 and GC376 are potent inhibitors of SARS-CoV-2 replication in cell culture. They are strong drug candidates for the treatment of human coronavirus infections because they have already been successful in animals. The work here lays the framework for their use in human trials for the treatment of COVID-19.
Предметные рубрики MeSH
A549 CellsAnimalsAntiviral AgentsBetacoronavirusBinding SitesChlorocebus aethiopsCoronavirus 3C ProteasesCoronavirus, FelineCrystallography, X-RayCysteine EndopeptidasesCytopathogenic Effect, ViralDrug RepositioningHumansInhibitory Concentration 50Molecular StructureProdrugsProtease InhibitorsPyrrolidinesSevere acute respiratory syndrome-related coronavirusSARS-CoV-2Sulfonic AcidsVero CellsViral Nonstructural ProteinsVirus ReplicationLactamsLeucine