Abstract: In contrast, V116A, I117V, E119A, and N295S substitutions resulted in significantly lower viral titers (1.2 logs) than the parental CA/04 virus in NHBE cells.
Abstract: The efficiencies of NAs with E119A, H275Y, and N295S mutations to catalyze all substrates were ~19.4% of the CA/04 NA.
Abstract: We compared the impact of V116A and I117V on the functional properties of NA and compared these mutations with that of previously reported NAI-resistant mutations, E119A,
Screening for Neuraminidase Inhibitor Resistance Markers among Avian Influenza Viruses of the N4, N5, N6, and N8 Neuraminidase Subtypes.
Abstract: Substitutions conferring NAI resistance were mainly categorized as either novel NA subtype specific (G/N147V/I, A246V, and I427L) or previously reported in other subtypes (E119A/D/V, Q136K, E276D, R292K, and R371K).
Clinical management and viral genomic diversity analysis of a child's influenza A(H1N1)pdm09 infection in the context of a severe combined immunodeficiency.
Method: We analyzed for the presence of NA substitutions associated with either NAI-resistant genotype in different NA subtypes (E119V/I/A/G, H274Y, R292K, and N294S: N2 numbering) or reduced susceptibility genotype to NAIs (Q136K, D151E/V/D, D198N/G/E/Y, I222V/T/K/R/M, S246N, E276D, and R371K: N2 numbering) among influenza A and B viruses.
Profiling and characterization of influenza virus N1 strains potentially resistant to multiple neuraminidase inhibitors.
Abstract: Of the 14 single and double mutant viruses recovered in the backbone of pH1N1, four variants (E119D, E119A/D/G-H274Y) exhibited reduced inhibition by all of the NAIs and two variants (E119D and E119D-H274Y) retained the overall properties of gene stability, replicative efficiency, pathogenicity, and transmissibility in vitro and in vivo.
Abstract: We therefore screened a known mutation(s) that could confer multidrug resistance to the currently approved NAIs oseltamivir, zanamivir, and peramivir by assessing recombinant viruses with mutant NA-encoding genes (catalytic residues R152K and R292K, framework residues <
Competitive fitness of influenza B viruses with neuraminidase inhibitor-resistant substitutions in a coinfection model of the human airway epithelium.
Abstract: Based on the lack of attenuated replication of rg-E119A in NHBE cells in the presence of oseltamivir or zanamivir and the fitness advantage of rg-H274Y over rg-WT, we emphasize the importance of these substitutions in the NA glycoprotein.
Abstract: Human infections with influenza B viruses carrying the E119A or H274Y substitution could limit the therapeutic options for those infected; the emergence of such viruses should be closely monitored.
Abstract: In a fluorescence-based assay, detection of rg-E119A was easily masked by the presence of NAI-susceptible virus.
Abstract: The replication in NHBE cells of viruses with reduced inhibition by oseltamivir (recombinant virus with the E119A
Study of oseltamivir and zanamivir resistance-related mutations in influenza viruses isolated from wild mallards in Sweden.
Method: The literature describing NAI resistance mutations has been reviewed, whereupon nine OC (V116A, I117V, E119V, D198N, I222V, H274Y, R292K, N294S and
Discussion: In the case of H5N1 2.2 A/Turkey/15/06 recombinant virus and inhibition by OC the IC50 for E119A, H274Y and N294S were 236.5, 6308.0 and 424.2 nM respectively (FL assay).
Discussion: The inhibition by ZA of the same recombinant virus that has V116A or E119A mutation resulted in IC50 of 32.8 and 1253.8 nM respectively.
Fitness costs for Influenza B viruses carrying neuraminidase inhibitor-resistant substitutions: underscoring the importance of E119A and H274Y.
PMID: 24566185
2014
Antimicrobial agents and chemotherapy
Abstract: Our results showed that four NA substitutions (D198E, I222T, H274Y, and N294S) conferred reduced inhibition by oseltamivir and three (E119A, D198Y, and R371K) conferred highly reduced inhibition by oseltamivir, zanamivir, and peramivir.
Abstract: Overall, viruses with the E119A or H274Y NA substitution possess fitness comparable to NAI-susceptible virus, and the acquisition of these substitutions by influenza B viruses should be closely monitored.
Abstract: Viruses with the E119A, I2
Characterization of drug-resistant influenza virus A(H1N1) and A(H3N2) variants selected in vitro with laninamivir.
PMID: 24957832
2014
Antimicrobial agents and chemotherapy
Abstract: In vitro, laninamivir pressure selected the E119A NA substitution in the A/Solomon Islands/3/2006 A(H1N1) background, whereas E119K and G147E NA changes along with a K133E hemagglutinin (HA) substitution were selected in the A/Quebec/144147/2009 A(H1N1)pdm09 strain.
IV mutation literature information.
PMID: 
2020
Antiviral research
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