Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300
David A. Davis, Haydar Bulut, Prabha Shrestha, Amulya Yaparla, Hannah K. Jaeger, Shin‐ichiro Hattori, Paul T. Wingfield, John J. Mieyal, Hiroaki Mitsuya, Robert Yarchoan
Abstract
activity by blocking its dimerization. This provides a novel accessible and reactive target for drug development. Moreover, this process may have implications for disease pathophysiology in humans and bats. It may be a mechanism by which SARS-CoV-2 has evolved to limit replication and avoid killing host bats when they are under oxidative stress during flight.
Topics & Concepts
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Coronavirus disease 2019 (COVID-19)2019-20 coronavirus outbreakPandemicCoronavirusProteaseCysteine proteaseCysteineBetacoronavirusCoronavirus InfectionsVirologySevere acute respiratory syndrome coronavirusChemistryBiologyEnzymeBiochemistryMedicineInfectious disease (medical specialty)OutbreakDiseasePathologySulfur Compounds in BiologyPhagocytosis and Immune RegulationSynthesis and Characterization of Heterocyclic Compounds