Method: For the genotypic analysis, mutations of amino acid regions related to drug resistance (E119V, R152K, H274Y, R292K, and N294S) were examined, via sequence analysis of NA gene.
Result: NA gene analysis was conducted on influenza viruses isolated from 51 patients (group A, 29 patients; group B, 22 patients) during the first study period in order to examine the drug resistance-related mutation of NA inhibitor (E119V, R152K, H274Y, R292K, N294S).
Simultaneous detection of oseltamivir- and amantadine-resistant influenza by oligonucleotide microarray visualization.
Discussion: For instance, I117V, I117M, S247N, I223R, N294S, and R292K of NA have been reported to be associated with NA inhibitor resistance, and some of them had combinatorial, compensatory, or synergistic effects.
Molecular basis of drug resistance in A/H1N1 virus.
PMID: 22978683
2012
Journal of chemical information and modeling
Abstract: In this study, free-energy perturbation was used to evaluate the relative binding free energies of Tamiflu and Relenza with H274Y, N294S, and Y252H neuraminidase mutants.
Study of Tamiflu sensitivity to variants of A/H5N1 virus using different force fields.
PMID: 21834591
2011
Journal of chemical information and modeling
Abstract: GROMOS96 43a1 provides a lower correlation as it supports Oseltamivir to be more resistant to N294S than H274Y.
Abstract: In this paper, we consider the impact of four main force fields, AMBER99SB, CHARMM27, GROMOS96 43a1, and OPLS-AA/L, on the binding affinity of Oseltamivir carboxylate to the wild-type and Y252H, N294S, and H274Y mutants of glycoprotein neuraminidase from the pandemic A/H5N1 virus.
Abstract: They correctly capture the binding ranking Y252H WT N294S H274Y observed in experiments (Collins, P.
Neuraminidase inhibitor R-125489--a promising drug for treating influenza virus: steered molecular dynamics approach.
PMID: 21693105
2011
Biochemical and biophysical research communications
Abstract: Based on results obtained by SMD and the molecular mechanics-Poisson-Boltzmann surface area method, we predict that R-125489 can be used to treat not only wild-type but also tamiflu-resistant N294S, H274Y variants of A/H5N1 virus as its binding affinity does not vary much across these systems.
An influenza A(H5N8) virus isolated during an outbreak at a poultry farm in Russia in 2017 has an N294S substitution in the neuraminidase and shows reduced susceptibility to oseltamivir.
Abstract: Although NA N294S-possessing H5N1 viruses were attenuated in mice and ferrets compared to their oseltamivir-sensitive counterparts, one of the infected ferrets died from systemic infection, demonstrating the potential lethality in ferrets of oseltamivir-resistant H5N1 viruses with the NA N294S substitution.
Abstract: Here, we assessed the effect of the NA N294S substitution on the replication and pathogenicity of human H5N1 viruses and on the efficacy of the NA inhibitors oseltamivir and zanamivir in mouse and ferret models.
Abstract: However, unlike viruses with the NA H274Y mutation, the properties of viruses possessing
Oseltamivir-resistant influenza A and B viruses pre- and postantiviral therapy in children and young adults with cancer.
PMID: 21048522
2011
The Pediatric infectious disease journal
Abstract: One patient was infected with oseltamivir-resistant influenza B virus (IC50, 731.86 +- 155.12 nM) that harbored a N294S NA mutation, the first report of this mutation in influenza B viruses.
Introduction: E119V and N294S mutations occur in the framework region of the NA.
Introduction: Other mutations such as an asparagine to serine substitution at position 294 (N294S), have been reported in both N2- and N1-containing viruses; these mutations are associated with a greater loss of in vitro susceptibility to oseltamivir in N2 than in N1 viruses but strains possessing these mutations retain susceptibility to zanamivir.
Result: For patient 12, influenza B virus harboring an N294S mutat
Clinical importance and impact on the households of oseltamivir-resistant seasonal A/H1N1 influenza virus in healthy children in Italy.
Abstract: The influenza A virus-positive samples underwent neuraminidase gene analysis using pyrosequencing to identify mutations H275Y and N294 S in A/H1N1, and E119V, R292K, and N294 S in A/H3N2.
Result: The A influenza virus-positive samples underwent neuraminidase gene analysis using pyrosequencing to identify mutations H275Y and N294 S in A/H1N1, and E119V, R292K, and N294 S in A/H3N2.
Effect of neuraminidase inhibitor-resistant mutations on pathogenicity of clade 2.2 A/Turkey/15/06 (H5N1) influenza virus in ferrets.
Abstract: However, H5N1 viruses carrying the E119A or the N294S NA mutation were lethal to 1 of 3 inoculated animals and were associated with significantly higher virus titers (P<0.01) and inflammation in the lungs compared to the wild-type virus.
Abstract: We generated seven genetically stable recombinant clade 2.2 A/Turkey/15/06-like (H5N1) influenza viruses carrying NA mutations located either in the framework residues (E119A, H274Y, N294S) or in close proximity to the NA enzyme active site (V116A, I117V, K150N, Y252H).
Introduction: Despite a high degree
Computational studies of H5N1 influenza virus resistance to oseltamivir.
Abstract: Detailed analyses indicated that conformational change of E276 in the Pocket 1 region of NA is a key source of drug resistance in the H274Y mutant but not in the N294S mutant.
Abstract: We examined two resistant NA mutations, H274Y and N294S, and one non-drug-resistant mutation, E119G.
IV mutation literature information.
PMID: 
2013
Korean journal of pediatrics
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