Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells

The main protease, M(pro), of SARS-CoV-2 is required to cleave the viral polyprotein into precise functional units for virus replication and pathogenesis. Here we demonstrate a quantitative reporter for M(pro) function in living cells, in which protease inhibition by genetic or chemical methods resu...

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Autores principales: Moghadasi, Seyad Arad, Becker, Jordan T., Belica, Christopher, Wick, Chloe, Brown, William L., Harris, Reuben S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7668733/
https://www.ncbi.nlm.nih.gov/pubmed/33200129
http://dx.doi.org/10.1101/2020.11.09.375139
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author Moghadasi, Seyad Arad
Becker, Jordan T.
Belica, Christopher
Wick, Chloe
Brown, William L.
Harris, Reuben S.
author_facet Moghadasi, Seyad Arad
Becker, Jordan T.
Belica, Christopher
Wick, Chloe
Brown, William L.
Harris, Reuben S.
author_sort Moghadasi, Seyad Arad
collection PubMed
description The main protease, M(pro), of SARS-CoV-2 is required to cleave the viral polyprotein into precise functional units for virus replication and pathogenesis. Here we demonstrate a quantitative reporter for M(pro) function in living cells, in which protease inhibition by genetic or chemical methods results in strong eGFP fluorescence. This robust gain-of-function system readily distinguishes between inhibitor potencies and can be scaled-up to high-throughput platforms for drug testing.
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spelling pubmed-76687332020-11-17 Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells Moghadasi, Seyad Arad Becker, Jordan T. Belica, Christopher Wick, Chloe Brown, William L. Harris, Reuben S. bioRxiv Article The main protease, M(pro), of SARS-CoV-2 is required to cleave the viral polyprotein into precise functional units for virus replication and pathogenesis. Here we demonstrate a quantitative reporter for M(pro) function in living cells, in which protease inhibition by genetic or chemical methods results in strong eGFP fluorescence. This robust gain-of-function system readily distinguishes between inhibitor potencies and can be scaled-up to high-throughput platforms for drug testing. Cold Spring Harbor Laboratory 2020-11-09 /pmc/articles/PMC7668733/ /pubmed/33200129 http://dx.doi.org/10.1101/2020.11.09.375139 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
spellingShingle Article
Moghadasi, Seyad Arad
Becker, Jordan T.
Belica, Christopher
Wick, Chloe
Brown, William L.
Harris, Reuben S.
Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title_full Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title_fullStr Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title_full_unstemmed Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title_short Gain-of-function assay for SARS-CoV-2 M(pro) inhibition in living cells
title_sort gain-of-function assay for sars-cov-2 m(pro) inhibition in living cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7668733/
https://www.ncbi.nlm.nih.gov/pubmed/33200129
http://dx.doi.org/10.1101/2020.11.09.375139
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