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The development of papain‐like protease from SARS‐CoV‐2, a potential drug target for antiviral screening: A review

Indonesian Journal of Biotechnology · Vol. 28 No. 3 (2023) · hlm. 158–172

DOI
10.22146/ijbiotech.83376
ISSN
2089-2241, 0853-8654
Terbit
2023-09-30
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

The SARS‐CoV‐2 outbreak caused a global pandemic, claiming numerous lives and becoming this century’s most widespread life‐threatening disease. The virus relies on two specific enzymes to facilitate replication, 3‐chymotrypsin‐like protease (3CLPro) and papain‐like protease (PLpro). These enzymes are crucial in breaking down nonstructural polypeptides into functional proteins. PLpro with LXGG↓X recognition and cleavage sites also play a role in deubiquitylase (DUB) and delSGylase by cleaving after the double glycine residue of ubiquitin (Ub) and ISG15 as a mechanism to suppress the host’s innate immune response. Despite its important role in the viral infection cycle and the potential for drug discovery, no antivirals have been approved as PLpro inhibitors. Therefore, this review focuses on PLpro protein, its recombinant product development and purification, and its application as a protein target in drug discovery for COVID‐19 screening to develop effective COVID‐19 drugs.

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Sumber metadata: OAI-PMH (metadata jurnal) https://jurnal.ugm.ac.id/ijbiotech/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en-US">The development of papain‐like protease from SARS‐CoV‐2, a potential drug target for antiviral screening: A review</dc:title>
	<dc:creator>Napitupulu, Riswanto</dc:creator>
	<dc:creator>Helianti, Is</dc:creator>
	<dc:creator>Maimunah, Maimunah</dc:creator>
	<dc:creator>Fatiningtyas, Fairuz Andini</dc:creator>
	<dc:creator>Malik, Amarila</dc:creator>
	<dc:subject xml:lang="en-US">Drug discovery; Papain‐like protease; SARS‐CoV‐2</dc:subject>
	<dc:description xml:lang="en-US">The SARS‐CoV‐2 outbreak caused a global pandemic, claiming numerous lives and becoming this century’s most widespread life‐threatening disease. The virus relies on two specific enzymes to facilitate replication, 3‐chymotrypsin‐like protease (3CLPro) and papain‐like protease (PLpro). These enzymes are crucial in breaking down nonstructural polypeptides into functional proteins. PLpro with LXGG↓X recognition and cleavage sites also play a role in deubiquitylase (DUB) and delSGylase by cleaving after the double glycine residue of ubiquitin (Ub) and ISG15 as a mechanism to suppress the host’s innate immune response. Despite its important role in the viral infection cycle and the potential for drug discovery, no antivirals have been approved as PLpro inhibitors. Therefore, this review focuses on PLpro protein, its recombinant product development and purification, and its application as a protein target in drug discovery for COVID‐19 screening to develop effective COVID‐19 drugs.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US">Riswanto Napitupulu/Maimunah/Fairuz Andini Fatiningtyas/Amarila Malik, Universitas Indonesia</dc:contributor>
	<dc:contributor xml:lang="en-US">Is Helianti, Research Center of Applied Microbiology BRIN</dc:contributor>
	<dc:date>2023-09-30</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en-US">Original Research Articles</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ugm.ac.id/ijbiotech/article/view/83376</dc:identifier>
	<dc:identifier>10.22146/ijbiotech.83376</dc:identifier>
	<dc:source xml:lang="en-US">Indonesian Journal of Biotechnology; Vol 28, No 3 (2023); 158-172</dc:source>
	<dc:source>2089-2241</dc:source>
	<dc:source>0853-8654</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/view/83376/37478</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26050</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26052</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26053</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26073</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26074</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26075</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/downloadSuppFile/83376/26076</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2023 The Author(s)</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
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