Antiviral activity of broad-spectrum and enterovirus-specific inhibitors against clinical isolates of enterovirus D68
| Autor: | Sun, Liang, Meijer, Adam, Froeyen, Mathy, Zhang, Linlin, Thibaut, Hendrik Jan, Baggen, Jim, George, Shyla, Vernachio, John, van Kuppeveld, Frank J M, Leyssen, Pieter, Hilgenfeld, Rolf, Neyts, Johan, Delang, Leen, LS Virologie, dI&I I&I-1 |
|---|---|
| Přispěvatelé: | LS Virologie, dI&I I&I-1 |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Receptors Drug Coronacrisis-Taverne Enterovirus D Drug resistance Microbial Sensitivity Tests Favipiravir Biology medicine.disease_cause Virus Replication Antiviral Agents Microbiology chemistry.chemical_compound Broad spectrum Viral Proteins Drug Resistance Viral medicine Enterovirus Infections Humans Pharmacology (medical) Oxazoles Respiratory Tract Infections Pharmacology Enterovirus D Human Oxadiazoles Pleconaril Virology Infectious Diseases chemistry Viral replication Enterovirus Enterovirus D68 |
| Zdroj: | Antimicrobial Agents and Chemotherapy, 59(12), 7782. American Society for Microbiology |
| ISSN: | 0066-4804 |
| Popis: | We investigated the susceptibility of 10 enterovirus D68 (EV-D68) isolates (belonging to clusters A, B, and C) to (entero)virus inhibitors with different mechanisms of action. The 3C-protease inhibitors proved to be more efficient than enviroxime and pleconaril, which in turn were more effective than vapendavir and pirodavir. Favipiravir proved to be a weak inhibitor. Resistance to pleconaril maps to V69A in the VP1 protein, and resistance to rupintrivir maps to V104I in the 3C protease. A structural explanation of why both substitutions may cause resistance is provided. ispartof: Antimicrobial Agents and Chemotherapy vol:59 issue:12 pages:7782-5 ispartof: location:United States status: published |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|