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3c Syndrome - Crossref

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Last Updated: 10 June 2022

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Assessing Activity and Inhibition of Middle East Respiratory Syndrome Coronavirus Papain-Like and 3C-Like Proteases Using Luciferase-Based Biosensors

"ABSTRACT Middle East respiratory syndrome coronavirus is linked to a rash of more than 90 cases of severe pneumonia with high mortality. " To quickly identify potential inhibitors of MERS-CoV replication, we presented the papain-like protease and the 3-chymotrypsin-like protease from MERS-CoV and developed luciferase biosensors in cells. We show that the ex MERS-CoV PLpro recognizes and processes the canonical CoV-PLPRO cleavage site RLKGG in the biosensor. However, current CoV PLpro inhibitors were unable to prevent MERS-CoV PLpro production, owing to the divergence of the amino acid sequence in the drug binding site. Importantly, we discovered that a small-molecule inhibitor that prevents replication of severe acute respiratory disease CoV and murine CoV has also reduced the production of MERS-CoV 3CLpro. Overall, the protease expression and biosensor assays developed here enable for rapid analysis of viral protease activity and the identification of protease inhibitors. ".

Source link: https://doi.org/10.1128/jvi.02105-13


Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease

"ABSTRACT Unlike 3C protease, the acute respiratory syndrome coronavirus 3C-like protease is only enzymatically active as a homodimer, and its catalysis is strictly limited by the peculiar extra domain. " Despite extensive research, two mysteries remain: how the dimer-monomer switch is controlled and why dimerization is absolutely required for catalysis. Here we present the monomeric crystal structure of the SARS-CoV3C4 mutant R298A with a resolution of 1. 75 Au030a. Dimerization seems to be linked to catalysis in 3CLpro, according to one network for dimerization and the other for catalysis. ".

Source link: https://doi.org/10.1128/jvi.02680-07


Cinanserin Is an Inhibitor of the 3C-Like Proteinase of Severe Acute Respiratory Syndrome Coronavirus and Strongly Reduces Virus Replication In Vitro

"ABSTRACT" is a blocker on "ABSTRACT" due to its vital role in the viral life cycle, the 3C-like proteinase of severe acute respiratory syndrome-associated coronavirus in the 3C-like proteinase is one of the most promising anti-SARS-CoV drugs. Surface plasmon resonance techniques demonstrated binding of both cinanserin and its hydrochloride to bacterially expressed 3CL pro of SARS-CoV and the related human coronavirus 229E. In tissue culture assays, namely, a replicon system based on HCoV-229E and quantitative test assays with infectious SARS-CoV and HCoV-229E were both tested, and experimental test assays with infectious SARS-CoV and HCoV-229E were further investigated. All assays revealed a significant inhibition of coronavirus replication at non-toxic drug levels. With IC 50 values ranging from 19 to 34 bcM, the number of virus RNA and infectious particles was reduced by up to four log units.

Source link: https://doi.org/10.1128/jvi.79.11.7095-7103.2005


Genetic Screen for Monitoring Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease

"ABSTRACT" explains "AbSTRACT="British coronavirus is the etiological agent of severe acute respiratory disease. Since SCoV, the main protease of drug therapy, has also been described as 3C-like protease, is a popular drug target for drug therapy, we have developed a safe, simple, and rapid genetic screen assay to track the SCoV 3C-like protease's activity. P1/P2 - A specific target for the SCoV 3C-like protease, P1/P2 repressor was introduced into the lambda phage cI repressor. The SCoV P1/P2 repressor's specificity was determined by coexpression of this repressor with a chemically synthesized SCoV 3C-like protease gene construct. The cI is encoded by two plasmids in Escherichia coli cells encoding the cI. Lambda phage cells that did not have the SCoV 3C-like protease were reproduced up to 2,000 fold more efficiently than cells that did not contain the SCoV 3C-like protease, according to the u03b2-galactosidase-SCoV 3C-like protease.

Source link: https://doi.org/10.1128/jvi.78.24.14057-14061.2004

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions