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Characterization and Noncovalent Inhibition of the Deubiquitinase and deISGylase Activity of SARS-CoV-2 Papain-Like Protease

ACS Infect Dis. 2020-06; 
Brendan T Freitas , Ian A Durie , Jackelyn Murray , Jaron E Longo , Holden C Miller , David Crich , Robert Jeff Hogan , Ralph A Tripp , Scott D Pegan
Products/Services Used Details Operation
PCR Cloning and Subcloning The ubiquitin-like domain (UbL) and the catalytic core of SARS-CoV-2 PLpro (orf1ab 1564-1876; 1-315) were cloned into pET-15b by Genscript and transformed into T7 express E. coli. Get A Quote

摘要

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent for COVID-19, is a novel human betacoronavirus that is rapidly spreading worldwide. The outbreak currently includes over 3.7 million cases and 260,000 fatalities. As a betacoronavirus, SARS-CoV-2 encodes for a papain-like protease (PLpro) that is likely responsible for cleavage of the coronavirus (CoV) viral polypeptide. The PLpro is also responsible for suppression of host innate immune responses by virtue of its ability to reverse host ubiquitination and ISGylation events. Here, the biochemical activity of SARS-CoV-2 PLpro against ubiquitin (Ub) and interferon-stimulated gene product 15 (ISG15) substrates is evaluated, revealing... More

关键词

COVID-19; ISG5; PLpro; coronavirus; severe acute respiratory syndrome 2; ubiquitin.