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Targeting novel structural and functional features of coronavirus protease nsp5 (3CLpro, Mpro) in the age of COVID-19
Author(s) -
Molly K. Roe,
Nathan A. Junod,
Audrey R. Young,
Dia C. Beachboard,
Christopher C. Stobart
Publication year - 2021
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/jgv.0.001558
Subject(s) - polyproteins , protease , coronavirus , biology , virology , covid-19 , coronaviridae , computational biology , enzyme , medicine , biochemistry , infectious disease (medical specialty) , disease , pathology , outbreak
Coronavirus protease nsp5 (M pro , 3CL pro ) remains a primary target for coronavirus therapeutics due to its indispensable and conserved role in the proteolytic processing of the viral replicase polyproteins. In this review, we discuss the diversity of known coronaviruses, the role of nsp5 in coronavirus biology, and the structure and function of this protease across the diversity of known coronaviruses, and evaluate past and present efforts to develop inhibitors to the nsp5 protease with a particular emphasis on new and mostly unexplored potential targets of inhibition. With the recent emergence of pandemic SARS-CoV-2, this review provides novel and potentially innovative strategies and directions to develop effective therapeutics against the coronavirus protease nsp5.

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