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SARS-CoV-2 Papain-Like Protease: Structure, Function and Inhibition

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dc.contributor.authorUllrich, Sven
dc.contributor.authorNitsche, Christoph
dc.date.accessioned2022-10-31T04:03:05Z
dc.date.available2022-10-31T04:03:05Z
dc.date.issued2022
dc.description.abstractEmerging variants of SARS-CoV-2 and potential novel epidemic coronaviruses underline the importance of investigating various viral proteins as potential drug targets. The papain-like protease of coronaviruses has been less explored than other viral proteins; however, its substantive role in viral replication and impact on the host immune response make it a suitable target to study. This review article focuses on the structure and function of the papain-like protease (PLpro ) of SARS-CoV-2, including variants of concern, and compares it to those of other coronaviruses, such as SARS-CoV-1 and MERS-CoV. The protease's recognition motif is mirrored in ubiquitin and ISG15, which are involved in the antiviral immune response. Inhibitors, including GRL0617 derivatives, and their prospects as potential future antiviral agents are also discussed.en_AU
dc.description.sponsorshipCN gratefully acknowledges funding by the Australian Research Council (DECRA: DE190100015; Discovery Project: DP200100348). The authors gratefully acknowledge Junming He (Australian National University) who designed and created the artwork for the frontispieceen_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.issn1439-4227en_AU
dc.identifier.urihttp://hdl.handle.net/1885/276813
dc.language.isoen_AUen_AU
dc.provenanceThis is an open access article under the terms of the Creative Commons Attribution Non-Commercial NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is noncommercial and no modifications or adaptations are madeen_AU
dc.publisherWileyen_AU
dc.relationhttp://purl.org/au-research/grants/arc/DE190100015en_AU
dc.relationhttp://purl.org/au-research/grants/arc/DP200100348en_AU
dc.rights© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbHen_AU
dc.rights.licenseCreative Commons Attribution-NonCommercial-NoDerivs Licenseen_AU
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en_AU
dc.sourceChembiochem : a European journal of chemical biologyen_AU
dc.subjectcovid-19en_AU
dc.subjectantiviralsen_AU
dc.subjectimmune responseen_AU
dc.subjectposttranslational modificationsen_AU
dc.subjectprotease inhibitorsen_AU
dc.subjectaniline compoundsen_AU
dc.subjectantiviral agentsen_AU
dc.subjectbenzamidesen_AU
dc.subjectcoronavirus papain-like proteasesen_AU
dc.subjecthumansen_AU
dc.subjectnaphthalenesen_AU
dc.subjectpeptide hydrolasesen_AU
dc.subjectprotease inhibitorsen_AU
dc.subjectsars-cov-2en_AU
dc.subjectubiquitinen_AU
dc.subjectviral proteinsen_AU
dc.subjectcovid-19en_AU
dc.subjectpapainen_AU
dc.titleSARS-CoV-2 Papain-Like Protease: Structure, Function and Inhibitionen_AU
dc.typeJournal articleen_AU
dcterms.accessRightsOpen Accessen_AU
local.bibliographicCitation.issue19en_AU
local.bibliographicCitation.startpagee202200327en_AU
local.contributor.affiliationUllrich, S., Research School of Chemistry, The Australian National Universityen_AU
local.contributor.affiliationNitsche, C., Research School of Chemistry, The Australian National Universityen_AU
local.identifier.citationvolume23en_AU
local.identifier.doi10.1002/cbic.202200327en_AU
local.identifier.essn1439-7633en_AU
local.publisher.urlhttps://www.wiley.com/en-gben_AU
local.type.statusPublished Versionen_AU

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