About: Application of a cell-based protease assay for testing inhibitors of picornavirus 3C proteases

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About: Application of a cell-based protease assay for testing inhibitors of picornavirus 3C proteases Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Application of a cell-based protease assay for testing inhibitors of picornavirus 3C proteases
Creator	Liu, Hong Hilgenfeld, Rolf Neyts, Johan De Clercq, Kris George, Shyla Kusov, Yuri Lacroix, Céline Ulferts, Rachel Goris, Nesya Lefebvre, David Lanke, Kjerstin Van Der Linden, Lonneke Van Kuppeveld, Frank Nabuurs, Sander
source	Elsevier; Medline; PMC
abstract	Abstract Proteolytical cleavage of the picornaviral polyprotein is essential for viral replication. Therefore, viral proteases are attractive targets for anti-viral therapy. Most assays available for testing proteolytical activity of proteases are performed in vitro, using heterologously expressed proteases and peptide substrates. To deal with the disadvantages associated with in vitro assays, we modified a cell-based protease assay for picornavirus proteases. The assay is based on the induction of expression of a firefly luciferase reporter by a chimeric transcription factor in which the viral protease and cleavage sites are inserted between the GAL4 binding domain and the VP16 activation domain. Firefly luciferase expression is dependent on cleavage of the transcription factor by the viral protease. This biosafe assay enables testing the effect of compounds on protease activity in cells while circumventing the need for infection. We designed the assay for 3C proteases (3Cpro) of various enteroviruses as well as of viruses of several other picornavirus genera, and show that the assay is amenable for use in a high-throughput setting. Furthermore, we show that the spectrum of activity of 3Cpro inhibitor AG7088 (rupintrivir) not only encompasses enterovirus 3Cpro but also 3Cpro of foot-and-mouth disease virus (FMDV), an aphthovirus. In contrary, AG7404 (compound 1), an analogue of AG7088, had no effect on FMDV 3Cpro activity, for which we provide a structural explanation.
has issue date	2014-03-31(xsd:dateTime)
bibo:doi	10.1016/j.antiviral.2013.12.012
bibo:pmid	24393668
has license	els-covid
sha1sum (hex)	23e1bfb13e7ba21c876bd7ed1de2f6b6770f1490
schema:url	https://doi.org/10.1016/j.antiviral.2013.12.012
resource representing a document's title	Application of a cell-based protease assay for testing inhibitors of picornavirus 3C proteases
has PubMed Central identifier	PMC7113757
has PubMed identifier	24393668
schema:publication	Antiviral Research
resource representing a document's body	covid:23e1bfb13e7ba21c876bd7ed1de2f6b6770f1490#body_text
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