Persistent Infection of Drug-resistant Influenza A Virus during Chemotherapy for Malignant Lymphoma.
PMID: 27374689
2016
Internal medicine (Tokyo, Japan)
Abstract: Virological analyses revealed that he was infected with the NA inhibitor-resistant A (H3N2) virus possessing an R292K substitution in the NA protein.
Human Monoclonal Antibody 81.39a Effectively Neutralizes Emerging Influenza A Viruses of Group 1 and 2 Hemagglutinins.
Low replicative fitness of neuraminidase inhibitor-resistant H7N9 avian influenza a virus with R292K substitution in neuraminidase in cynomolgus macaques compared with I222T substitution.
PMID: 27714494
2016
Journal of computer-aided molecular design
Abstract: However, some H7N9 strains that have been isolated from patient after drug treatment have a R292K mutation in neuraminidase.
Abstract: In addition, oseltamivir does not bind well to the R292K mutant complex as shown by the high degree of fluctuation in ligand RMSD during the simulation and the change in angular distribution of bulky side chain groups.
Identification of novel compounds against an R294K substitution of influenza A (H7N9) virus using ensemble based drug virtual screening.
PMID: 25589893
2015
International journal of medical sciences
3Introduction: Single amino acid change known as the ""H275Y"" mutation in 2009 H1N1 flu virus and ""R292K"" mutation in influenza A virus is conferred by drug resistance."
Introduction: Orientation and stabilization of various inhibitors in NA protein depend major on two or three Arginine residues in 150 loop, R292K mutation succeeded to unbalance stability and orientation of these inhibitors leading to drug resistance.
Result: The docking results of H7N9 NA agreed well with the experiential results in which NA R292K substitution was highly resistant to Oseltamivir and Peramivir and partially resistant to Zanamivir.
Neuraminidase Mutations Conferring Resistance to Oseltamivir in Influenza A(H7N9) Viruses.
Abstract: Collectively, we demonstrate that R292K, E119V, and I222K reduced the inhibitory activity of oseltamivir, not only in the NI assay, but also in infected ferrets, judged particularly by viral loads in nasal washes, and may signal the need for alternative therapeutics.
Abstract: Conversely, treatment failed to significantly inhibit the replication of R292K or E119V virus.
Abstract: In the NA inhibition (NI) assay, R292K conferred highly reduced inhibition by oseltamivir, while E119V and I222K each caused reduced inhibition.
Abstract: The propensity for oseltamivir resistance emergence was assessed in oseltamivir-treated animals infected with wild-type
Amino acid substitutions in the neuraminidase protein of an H9N2 avian influenza virus affect its airborne transmission in chickens.
Discussion: reported that substitution of R292K in the NA of A/Sydney/5/97 weakened virus infectivity and abolished parental airborne transmissibility in ferrets.
Low replicative fitness of neuraminidase inhibitor-resistant H7N9 avian influenza a virus with R292K substitution in neuraminidase in cynomolgus macaques compared with I222T substitution.
Abstract: CONCLUSIONS: Discrepancies in the proportion of R292K variants between clinical samples and isolates should be suspected in clinical settings.
Abstract: Prior to treatment, R292K variants were detected in all clinical samples; however, they comprised only a small fraction of the total population.
Abstract: STUDY DESIGN: We measured the populations of the low-susceptibility influenza A H3N2 variants E119V and R292K by qRT-PCR using 305 nasal aspiration samples collected over time from 13, 16, and 11 patients treated with no neuraminidase inhibitors, oseltamivir, and zanamivir, respectively.
Abstract: The proportion of the R292K variant in clinical samples increased for 6/27 (22.2%) patients treated with oseltamivir or zanamivir, whereas an increase in the p
Low replicative fitness of neuraminidase inhibitor-resistant H7N9 avian influenza a virus with R292K substitution in neuraminidase in cynomolgus macaques compared with I222T substitution.
Abstract: AIM AND METHODS: In a previous in vivo Mallard experiment, an influenza A(H6N2) virus developed oseltamivir resistance by the R292K substitution in the neuraminidase (NA), when the birds were exposed to oseltamivir.
Abstract: Three variants of resistant H6N2/R292K virus were each propagated during 17 days in five successive pairs of naive Mallards, while oseltamivir exposure was decreased and removed.
Introduction: In addition to the R292K substitution, also the D113N and D141N substitutions of unknown significance were observed in NA.
Introduction: In an H10N8 virus though, despite classed as group N1 neuraminidase, NAI
Influenza A viruses of swine circulating in the United States during 2009-2014 are susceptible to neuraminidase inhibitors but show lineage-dependent resistance to adamantanes.
Method: (accessed 10/23/2014) were screened for the presence of known molecular markers (N2 numbering) of NAI resistance that demonstrated clinical relevance in human influenza A viruses of N1 (D198N, I222R, H274Y, N294S) or N2 (E119V, R292K, N294S) subtypes, and for NA markers reported in surveillance studies or in recombinant viruses of N1 (V116A, I117V, E119V, Q136L/K, V149A, Y155H, I222V/M/K,
Unique Determinants of Neuraminidase Inhibitor Resistance among N3, N7, and N9 Avian Influenza Viruses.
Abstract: In a fluorescence-based NA inhibition assay, we identified three categories of NA substitutions associated with reduced inhibition by NAIs (oseltamivir, zanamivir, and peramivir): (i) novel subtype-specific substitutions in or near the enzyme catalytic site (R152W, A246T, and D293N, N2 numbering), (ii) subtype-independent substitutions (E119G/V and/or D and R292K), and (iii) substitutions previously reported in other subtypes (Q136K, I222M, and E276D).
IV mutation literature information.
PMID: 
2016
Internal medicine (Tokyo, Japan)
Browser Board
Co-occurred Entities
Filtrator
ViMRT