Estimating the Fitness Advantage Conferred by Permissive Neuraminidase Mutations in Recent Oseltamivir-Resistant A(H1N1)pdm09 Influenza Viruses

• Main Authors: Butler J., Hooper K.A., Petrie S., Lee R., Maurer-Stroh S., Reh L., Guarnaccia T., Baas C., Xue L., Vitesnik S., Leang S.-K., McVernon J., Kelso A., Barr I.G., McCaw J.M., Bloom J.D., Hurt A.C.
• Other Authors: BIOLOGICAL SCIENCES
• Format: Article
• Published: 2019
• Subjects: DNA fragment; oseltamivir; virus sialidase; antivirus agent; NA protein, influenza A virus; sialidase; virus protein; 2009 H1N1 influenza; article; clinical article; clinical feature; controlled study; disease course; disease transmission; drug resistance; enzyme activity; enzyme inhibition assay; gene amplification; gene mutation; human; human cell; in vitro study; influenza; mathematical model; protein expression; quantitative analysis; reverse transcription polymerase chain reaction; RNA extraction; sequence analysis; site directed mutagenesis; virus replication; amino acid substitution; animal; antagonists and inhibitors; antiviral resistance; dog; ferret; genetics; Influenza virus A H1N1; Influenza, Human; MDCK cell line; missense mutation; reproductive fitness; Amino Acid Substitution; Animals; Antiviral Agents; Dogs; Drug Resistance, Viral; Ferrets; Genetic Fitness; Humans; Influenza A Virus, H1N1 Subtype; Madin Darby Canine Kidney Cells; Mutation, Missense; Neuraminidase; Oseltamivir; Viral Proteins
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/161953
• Institution: National University of Singapore

10.1371/journal.ppat.1004065