ArticleAntimicrobial agents and chemotherapy2015
Peptidyl aldehyde NK-1.8k suppresses enterovirus 71 and enterovirus 68 infection by targeting protease 3C.
Article in Antimicrobial agents and chemotherapy, 2015. 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, 41 citations in OpenAlex.
- Review
- From the "One-Molecule, One-Target, One-Disease" Concept towards Looking for Multi-Target Therapeutics for Treating Non-Polio Enterovirus (NPEV) Infections.Pharmaceuticals (Basel, Switzerland) · 2024Review
- The nucleoside analog 4'-fluorouridine suppresses the replication of multiple enteroviruses by targeting 3D polymerase.Antimicrobial agents and chemotherapy · 2024Article
- An orally bioavailable SARS-CoV-2 main protease inhibitor exhibits improved affinity and reduced sensitivity to mutations.Science translational medicine · 2024Article
- Advances in anti-EV-A71 drug development research.Journal of advanced research · 2024Review
- PRSC chemical biology · 2023Review
- Computational and experimental studies of salvianolic acid A targets 3C protease to inhibit enterovirus 71 infection.Frontiers in pharmacology · 2023Article
- Enterovirus A71 antivirals: Past, present, and future.Acta pharmaceutica Sinica. B · 2022Article
- Recent advances of enterovirus 71Virology journal · 2020Review
- The Function and Mechanism of Enterovirus 71 (EV71) 3C Protease.Current microbiology · 2020Review
- Activity-Based Protein Profiling Identifies ATG4B as a Key Host Factor for Enterovirus 71 Proliferation.Journal of virology · 2019Article
- Discovery of Potent EV71 Capsid Inhibitors for Treatment of HFMD.ACS medicinal chemistry letters · 2017Article
- Structure of the Enterovirus 71 3C Protease in Complex with NK-1.8k and Indications for the Development of Antienterovirus Protease Inhibitor.Antimicrobial agents and chemotherapy · 2017Article
- Suramin interacts with the positively charged region surrounding the 5-fold axis of the EV-A71 capsid and inhibits multiple enterovirus A.Scientific reports · 2017Article
- A Novel Enterovirus 71 (EV71) Virulence Determinant: The 69th Residue of 3C Protease Modulates Pathogenicity.Frontiers in cellular and infection microbiology · 2017Article
- Human Enterovirus 68 Interferes with the Host Cell Cycle to Facilitate Viral Production.Frontiers in cellular and infection microbiology · 2017Article
- Enterovirus D68 and Human Respiratory Infections.Seminars in respiratory and critical care medicine · 2016Review
- Review
- A Conserved Inhibitory Mechanism of a Lycorine Derivative against Enterovirus and Hepatitis C Virus.Antimicrobial agents and chemotherapy · 2016Article
- Antiviral Activity of Broad-Spectrum and Enterovirus-Specific Inhibitors against Clinical Isolates of Enterovirus D68.Antimicrobial agents and chemotherapy · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enterovirus (EV) is one of the major causative agents of hand, foot, and mouth disease in the Pacific-Asia region. In particular, EV71 causes severe central nervous system infections, and the fatality rates from EV71 infection are high. Moreover, an outbreak of respiratory illnesses caused by an emerging EV, EV68, recently occurred among over 1,000 young children in the United States and was also associated with neurological infections. Although enterovirus has emerged as a considerable global public health threat, no antiviral drug for clinical use is available. In the present work, we screened our compound library for agents targeting viral protease and identified a peptidyl aldehyde, NK-1.8k, that inhibits the proliferation of different EV71 strains and one EV68 strain and that had a 50% effective concentration of 90 nM. Low cytotoxicity (50% cytotoxic concentration, >200 μM) indicated a high selective index of over 2,000. We further characterized a single amino acid substitution inside protease 3C (3C(pro)), N69S, which conferred EV71 resistance to NK-1.8k, possibly by increasing the flexibility of the substrate binding pocket of 3C(pro). The combination of NK-1.8k and an EV71 RNA-dependent RNA polymerase inhibitor or entry inhibitor exhibited a strong synergistic anti-EV71 effect. Our findings suggest that NK-1.8k could potentially be developed for anti-EV therapy.
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