ArticleThe Biochemical journal2015
SARS hCoV papain-like protease is a unique Lys48 linkage-specific di-distributive deubiquitinating enzyme.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 75 citations in OpenAlex.
- Ubiquitination and autophagy in host-pathogen interactions: from immune surveillance to therapeutic targeting.Nature reviews. Immunology · 2026Review
- From molecular logic to therapeutic modulation: advances in Ub/UBL signalling.Essays in biochemistry · 2025Article
- Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025Article
- Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025Review
- A microsporidial deubiquitinase blocks ubiquitin transfer from adenylated E1 to human UBE2K ubiquitin conjugating enzyme.bioRxiv : the preprint server for biology · 2025Article
- Regulation of N-degron recognin-mediated autophagy by the SARS-CoV-2 PLpro ubiquitin deconjugase.Autophagy · 2025Article
- Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53.Nature chemical biology · 2025Article
- Role of marine natural products in the development of antiviral agents against SARS-CoV-2: potential and prospects.Marine life science & technology · 2024Review
- Deubiquitinating activity of SARS-CoV-2 papain-like protease does not influence virus replication or innate immune responses in vivo.PLoS pathogens · 2024Article
- What Strengthens Protein-Protein Interactions: Analysis and Applications of Residue Correlation Networks.Journal of molecular biology · 2023Article
- USP2 inhibition prevents infection with ACE2-dependent coronaviruses in vitro and is protective against SARS-CoV-2 in mice.Science translational medicine · 2023Article
- Entropy driven cooperativity effect in multi-site drug optimization targeting SARS-CoV-2 papain-like protease.Cellular and molecular life sciences : CMLS · 2023Article
- Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA.Molecular cell · 2023Article
- Direct Interaction of Coronavirus Nonstructural Protein 3 with Melanoma Differentiation-Associated Gene 5 Modulates Type I Interferon Response during Coronavirus Infection.International journal of molecular sciences · 2022Article
- Exploring Noncovalent Protease Inhibitors for the Treatment of Severe Acute Respiratory Syndrome and Severe Acute Respiratory Syndrome-Like Coronaviruses.ACS infectious diseases · 2022Article
- Structural and Biochemical Characterization of Porcine Epidemic Diarrhea Virus Papain-Like Protease 2.Journal of virology · 2022Article
- Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2.Molecular cell · 2021Article
- A molecular sensor determines the ubiquitin substrate specificity of SARS-CoV-2 papain-like protease.Cell reports · 2021Article
- EGCG, a Green Tea Catechin, as a Potential Therapeutic Agent for Symptomatic and Asymptomatic SARS-CoV-2 Infection.Molecules (Basel, Switzerland) · 2021Review
- Potential molecular targets of nonstructural proteins for the development of antiviral drugs against SARS-CoV-2 infection.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2021Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Ubiquitin (Ub) and the Ub-like (Ubl) modifier interferon-stimulated gene 15 (ISG15) participate in the host defence of viral infections. Viruses, including the severe acute respiratory syndrome human coronavirus (SARS hCoV), have co-opted Ub-ISG15 conjugation pathways for their own advantage or have evolved effector proteins to counter pro-inflammatory properties of Ub-ISG15-conjugated host proteins. In the present study, we compare substrate specificities of the papain-like protease (PLpro) from the recently emerged Middle East respiratory syndrome (MERS) hCoV to the related protease from SARS, SARS PLpro. Through biochemical assays, we show that, similar to SARS PLpro, MERS PLpro is both a deubiquitinating (DUB) and a deISGylating enzyme. Further analysis of the intrinsic DUB activity of these viral proteases revealed unique differences between the recognition and cleavage specificities of polyUb chains. First, MERS PLpro shows broad linkage specificity for the cleavage of polyUb chains, whereas SARS PLpro prefers to cleave Lys48-linked polyUb chains. Secondly, MERS PLpro cleaves polyUb chains in a 'mono-distributive' manner (one Ub at a time) and SARS PLpro prefers to cleave Lys48-linked polyUb chains by sensing a di-Ub moiety as a minimal recognition element using a 'di-distributive' cleavage mechanism. The di-distributive cleavage mechanism for SARS PLpro appears to be uncommon among USP (Ub-specific protease)-family DUBs, as related USP family members from humans do not display such a mechanism. We propose that these intrinsic enzymatic differences between SARS and MERS PLpro will help to identify pro-inflammatory substrates of these viral DUBs and can guide in the design of therapeutics to combat infection by coronaviruses.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.