ArticleJournal of molecular biology2017
Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
60 citing papers in PubMed, 122 citations in OpenAlex.
- Role of HWorld journal of clinical cases · 2022Trial
- Viral interferon antagonism shapes host tropism.PLoS pathogens · 2025Review
- ISG-15, beyond its functions in the cell: a mini review.Cellular and molecular life sciences : CMLS · 2025Review
- ISG15-Dependent Stabilisation of USP18 Is Necessary but Not Sufficient to Regulate Type I Interferon Signalling in Humans.European journal of immunology · 2025Article
- Site-selective photo-crosslinking for the characterisation of transient ubiquitin-like protein-protein interactions.PloS one · 2025Article
- Over time analysis of the codon usage of SARS-CoV-2 and its variants.Computational and structural biotechnology journal · 2025Article
- Deubiquitinating activity of SARS-CoV-2 papain-like protease does not influence virus replication or innate immune responses in vivo.PLoS pathogens · 2024Article
- The role of IBV PL1pro in virus replication and suppression of host innate immune responses.BMC veterinary research · 2023Article
- A covalent inhibitor targeting the papain-like protease from SARS-CoV-2 inhibits viral replication.RSC advances · 2023Article
- Characterization of the Ubiquitin and ISG15 Deconjugase Activity of SARS-CoV-1 and SARS-CoV-2 Papain-Like Protease.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The diverse repertoire of ISG15: more intricate than initially thought.Experimental & molecular medicine · 2022Review
- Amino acid variants of SARS-CoV-2 papain-like protease have impact on drug binding.PLoS computational biology · 2022Article
- Chalcone-amide, a privileged backbone for the design and development of selective SARS-CoV/SARS-CoV-2 papain-like protease inhibitors.European journal of medicinal chemistry · 2022Review
- Association between Mutations in Papain-like Protease (PLpro) of SARS-CoV-2 with COVID-19 Clinical Outcomes.Pathogens (Basel, Switzerland) · 2022Article
- Type-I interferons in the immunopathogenesis and treatment of Coronavirus disease 2019.European journal of pharmacology · 2022Review
- The Evolutionary Dance between Innate Host Antiviral Pathways and SARS-CoV-2.Pathogens (Basel, Switzerland) · 2022Review
- 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
- SARS-COV-2 Coronavirus Papain-like Protease PLpro as an Antiviral Target for Inhibitors of Active Site and Protein-Protein Interactions.Biophysics · 2022Article
- A 3D structural SARS-CoV-2-human interactome to explore genetic and drug perturbations.Nature methods · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) encode multifunctional papain-like proteases (PLPs) that have the ability to process the viral polyprotein to facilitate RNA replication and antagonize the host innate immune response. The latter function involves reversing the post-translational modification of cellular proteins conjugated with either ubiquitin (Ub) or Ub-like interferon-stimulated gene product 15 (ISG15). Ub is known to be highly conserved among eukaryotes, but surprisingly, ISG15 is highly divergent among animals. The ramifications of this sequence divergence to the recognition of ISG15 by coronavirus PLPs at a structural and biochemical level are poorly understood. Therefore, the activity of PLPs from SARS-CoV, MERS-CoV, and mouse hepatitis virus was evaluated against seven ISG15s originating from an assortment of animal species susceptible, and not, to certain coronavirus infections. Excitingly, our kinetic, thermodynamic, and structural analysis revealed an array of different preferences among PLPs. Included in these studies is the first insight into a coronavirus PLP's interface with ISG15 via SARS-CoV PLpro in complex with the principle binding domain of human ISG15 (hISG15) and mouse ISG15s (mISG15s). The first X-ray structure of the full-length mISG15 protein is also reported and highlights a unique, twisted hinge region of ISG15 that is not conserved in hISG15, suggesting a potential role in differential recognition. Taken together, this new information provides a structural and biochemical understanding of the distinct specificities among coronavirus PLPs observed and addresses a critical gap of how PLPs can interact with ISG15s from a wide variety of species.
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Registered trials
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.