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Characterization and noncovalent inhibition of the deubiquitinase and deISGylase activity of SARS-CoV-2 papain-like protease
Non-conventional in English | WHO COVID | ID: covidwho-324460
ABSTRACT
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 CoV viral poly-peptide. 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 and ISG15 substrates is evaluated revealing that the protease has a marked reduction in its ability to process K48 linked Ub substrates compared to its counter part in SARS-CoV. Additionally, its substrate activity more closely mirrors that of the PLpro from the Middle East respiratory syndrome coronavirus and prefers ISG15s from certain species including humans. Additionally, naphthalene based PLpro inhibitors are shown to be effective at halting SARS-CoV-2 PLpro activity as well as SARS-CoV-2 replication.
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Collection: Databases of international organizations Database: WHO COVID Type of study: Experimental Studies Language: English Document Type: Non-conventional

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Collection: Databases of international organizations Database: WHO COVID Type of study: Experimental Studies Language: English Document Type: Non-conventional