Abstract: We found that recombinant E119D and E119A/D/G/-H274Y mutant viruses demonstrated reduced inhibition by all of the NAIs tested in both the backbone
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.
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).
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)
Solid phase assay for comparing reactivation rates of neuraminidases of influenza wild type and resistant mutants after inhibitor removal.
Abstract: Viruses with H274Y, E119V and E119G mutations demonstrated faster dissociation of the inhibitor to which they were resistant.
Method: Stocks of the following viruses were grown in Madin Darby Canine Kidney Cells, (MDCK): A/Mississippi/03/01 H1N1 wild type and oseltamivir resistant H274Y mutant,, A/Fukui/45/04 H3N2 wild type and E119V oseltamivir resistant mutant, B/Perth/211/01 influenza B wild type and D197E mutant with decreased susceptibility to all NAIs, NWS/G70C H1N9 wild type and E119G mutant with decreased susceptibility to zanamivir and peramivir.
Result: For the E119G virus with high zanamivir resistance, dissociat
Insights into susceptibility of antiviral drugs against the E119G mutant of 2009 influenza A (H1N1) neuraminidase by molecular dynamics simulations and free energy calculations.
Abstract: However, for ZNV, the E119G mutation has both direct and indirect influences on the drug binding.
Abstract: In this study, molecular dynamics (MD) simulations and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) were applied to investigate the different sensitivities of oseltamivir (OTV), zanamivir (ZNV), and peramivir (PRV) against the E119G mutant of 2009 A/H1N1 neuraminidase.
Abstract: The indirectly conformational variations of the inhibitors, which caused by the E119G mutation, are responsible for the loss of the binding free energies.
Abstract: The predicted binding free energies indicate that the E119G mutation in NA confers resistance to all of the three studied inhibitors.
Generation and Characterization of Recombinant Influenza A(H1N1) Viruses Resistant to Neuraminidase Inhibitors.
PMID: 24524021
2013
Osong public health and research perspectives
Introduction: Other NA mutations (N2 numbering: E119G, H274Y, R292K, and N295S) that have been reported to confer resistance to NAIs were each introduced into recombinant A/Vietnam/1203/04(H5N1) influenza virus.
Effect of neuraminidase inhibitor-resistant mutations on pathogenicity of clade 2.2 A/Turkey/15/06 (H5N1) influenza virus in ferrets.
Introduction: Despite a high degree of conservation of these residues, the NA substitutions identified in NA inhibitor-resistant influenza viruses isolated both in vitro and clinically tend to be NA subtype-specific: E119A/G/D/V, R292K, and N294S in the N2 and N9 subtypes and H274Y and N294S in the N1 subtype.
Discussion:
Discussion: E119G/A/D/V NA mutations are commonly reported to be associated with NA inhibitor resistance and were identified in influenza viruses of the N2 NA subtype.
Computational studies of H5N1 influenza virus resistance to oseltamivir.
Abstract: We examined two resistant NA mutations, H274Y and N294S, and one non-drug-resistant mutation, E119G.
Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo.
Abstract: Four NA mutations (E119G, H274Y, R292K, and N294S) that have been reported to confer resistance to NA inhibitors were each introduced into recombinant A/Vietnam/1203/04 (VN1203) H5N1 influenza virus.
Abstract: The E119G and R292K mutations significantly compromised viral growth in vitro, but the H274Y and N294S mutations were stably maintained in VN1203 and PR8 viruses.
Mutations conferring zanamivir resistance in human influenza virus N2 neuraminidases compromise virus fitness and are not stably maintained in vitro.
PMID: 16891631
2006
The Journal of antimicrobial chemotherapy
Abstract: Those with E119G, E119A or R152K mutations could only be rescued in the presence of exogenous NA and after passage in the absence of exogenous NA only isolates that had reverted to the wild-type NA or, surprisingly, E119G/A to E119V NA were isolated.
IV mutation literature information.
PMID: 
2015
Journal of virology
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