Introduction: discovered a series of diazenylaryl sulfonic acids as NA inhibitors, which inhibited N1 NA with drug-resistant mutations, including H274Y, N294S, Y155H, Q136L, I427Q and I427M.
Result: It should be noted that these three new 150-cavity inhibitors were not located within the V4 anchor, which contains residues I222 and H274, suggesting that these inhibitors may not be affected by the two drug-resistant mutations R292K, N294S and H274Y.
Discussion: Mutations of residues in various anchor regions of NA, including E199V
Global update on the susceptibility of human influenza viruses to neuraminidase inhibitors, 2015-2016.
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.
Platform for determining the inhibition profile of neuraminidase inhibitors in an influenza virus N1 background.
PMID: 27659246
2016
Journal of virological methods
Abstract: Employing reverse genetics, a set of influenza virus variants containing an amino acid substitution associated with oseltamivir resistance in N1 isolates (H274Y, N294S, Y155H or Q136L) was generated.
Abstract: For 5-amidino and 5-guanidino analogs of oseltamivir a significantly stronger inhibition of virus variants carrying a NA-H274Y was confirmed, and additionally shown for NA-N294S and NA-Y155H substitutions as compared to the parent compound.
Abstract: Novel NAIs should in particular be also effective against seasonal and/or pandemic N1 that carry a H274Y
Residue-based design of small molecule inhibitor for H1N1, H5N1 and H7N1 mutants.
Abstract: Our in silico findings suggest that saussureamine C can inhibit H274Y and N294S mutants, and that diiodotyrosine can also inhibit N294S mutants.
Abstract: Point mutations H274Y and N294S can lead to resistance of influenza virus strains to some drug molecules.
Competitive fitness of influenza B viruses with neuraminidase inhibitor-resistant substitutions in a coinfection model of the human airway epithelium.
Abstract: The replication in NHBE cells of viruses with reduced inhibition by oseltamivir (recombinant virus with the E119A mutation generated by reverse genetics [rg-E119A], rg-D198E, rg-I222T, rg-H274Y, rg-N294S, and rg-R371K, N2 numbering) or zanamivir (rg-E119A and rg-R371K) failed to be inhibited by the presence of the respective NAI.
Abstract: We coinfected NHBE cells with NAI-susceptible and -resistant viruses and used next-generation deep sequencing to reveal the order of relative fitness compared to that of recombinant wild-type (WT) virus generated by reverse genetics (rg-WT): rg- PMID: 25701593
2015
Antiviral research
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,
Profiling and characterization of influenza virus N1 strains potentially resistant to multiple neuraminidase inhibitors.
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 E119A/D/G, D198N, H274Y, and N294S) in the backbones of the 2009 pandemic H1N1 (pH1N1) and highly pathogenic avian influenza (HPAI) H5N1 viruses.
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: Cell surface NA protein expression was significantly increased by H274Y and N294S substitutions.
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: Viruses with the E119A, I222T, H274Y, or N294S substitution were not attenuated in replication ef
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 I314V) and ten ZA (V116A, R118K, E119G/A/D, Q136K, D151E/G/N, R152K, R224K, E276D, R292K and R371K)
IV mutation literature information.
PMID: 
2017
Scientific reports
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