ArticleJournal of virology2011
Structural basis for antiviral inhibition of the main protease, 3C, from human enterovirus 93.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Structural insights into the antiviral efficacy of AG7404 against human rhinovirus 3C proteases.IUCrJ · 2026Article
- Virulence determinant of Senecavirus A: 3C protein functions as a protease to cleave viral polyprotein and host factors.Virulence · 2025Review
- Structural basis for 3C and 3CD recruitment by enteroviral genomes during negative-strand RNA synthesis.Nature communications · 2025Article
- Structure of coxsackievirus cloverleaf RNA and 3CScience advances · 2025Article
- Article
- Crystal structures of the 3C proteases from Coxsackievirus B3 and B4.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structure and inhibition of SARS-CoV-1 and SARS-CoV-2 main proteases by oral antiviral compound AG7404.Antiviral research · 2022Article
- Structural similarities between SARS-CoV2 3CLFrontiers in chemistry · 2022Article
- DWV InfectionFrontiers in microbiology · 2021Article
- Viral proteases: Structure, mechanism and inhibition.The Enzymes · 2021Article
- Structural Biology of the Enterovirus Replication-Linked 5'-Cloverleaf RNA and Associated Virus Proteins.Microbiology and molecular biology reviews : MMBR · 2020Review
- Article
- Endogenous Protease Inhibitors in Airway Epithelial Cells Contribute to Eosinophilic Chronic Rhinosinusitis.American journal of respiratory and critical care medicine · 2017Article
- Emerging Role of Proteases in the Pathogenesis of Chronic Rhinosinusitis with Nasal Polyps.Frontiers in cellular and infection microbiology · 2017Review
- A Novel Enterovirus 71 (EV71) Virulence Determinant: The 69th Residue of 3C Protease Modulates Pathogenicity.Frontiers in cellular and infection microbiology · 2017Article
- Coxsackievirus B3 protease 3C: expression, purification, crystallization and preliminary structural insights.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Irreversible inhibitors of the 3C protease of Coxsackie virus through templated assembly of protein-binding fragments.Nature communications · 2016Article
- Enteroviral proteases: structure, host interactions and pathogenicity.Reviews in medical virology · 2016Review
- Article
- 3C protease of enterovirus 68: structure-based design of Michael acceptor inhibitors and their broad-spectrum antiviral effects against picornaviruses.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the Enterovirus genus of the Picornaviridae family are abundant, with common human pathogens that belong to the rhinovirus (HRV) and enterovirus (EV) species, including diverse echo-, coxsackie- and polioviruses. They cause a wide spectrum of clinical manifestations ranging from asymptomatic to severe diseases with neurological and/or cardiac manifestations. Pandemic outbreaks of EVs may be accompanied by meningitis and/or paralysis and can be fatal. However, no effective prophylaxis or antiviral treatment against most EVs is available. The EV RNA genome directs the synthesis of a single polyprotein that is autocatalytically processed into mature proteins at Gln↓Gly cleavage sites by the 3C protease (3C(pro)), which has narrow, conserved substrate specificity. These cleavages are essential for virus replication, making 3C(pro) an excellent target for antivirus drug development. In this study, we report the first determination of the crystal structure of 3C(pro) from an enterovirus B, EV-93, a recently identified pathogen, alone and in complex with the anti-HRV molecules compound 1 (AG7404) and rupintrivir (AG7088) at resolutions of 1.9, 1.3, and 1.5 Å, respectively. The EV-93 3C(pro) adopts a chymotrypsin-like fold with a canonically configured oxyanion hole and a substrate binding pocket similar to that of rhino-, coxsackie- and poliovirus 3C proteases. We show that compound 1 and rupintrivir are both active against EV-93 in infected cells and inhibit the proteolytic activity of EV-93 3C(pro) in vitro. These results provide a framework for further structure-guided optimization of the tested compounds to produce antiviral drugs against a broad range of EV species.
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