Discussion: For H3N2 viruses, we did not detect the mutations conferring resistance to neuraminidase inhibitors such as E119V, D151E, I222V, R224K, E276D, N249S, R292K, and R371K in the NA gene segment of our H3N2 isolates.
Identification and Characterization of Novel Antibody Epitopes on the N2 Neuraminidase.
Abstract: However, molecular analysis revealed the E119V mutation in the NA gene and a human host marker mutation E382D in the polymerase acidic (PA) gene, implying their susceptibility to neuraminidase inhibitors and potential infectivity in humans, respectively.
Result: However, the E119V mutation in NA was detected in all H6N5 isolates, suggesting their susceptibility to neuraminidase inhibitors, such as Oseltamivir, Peramivir, and Zanamivir.
Table: E119V
A molecularly engineered antiviral banana lectin inhibits fusion and is efficacious against influenza virus infection in vivo.
Result: S1), in which NA inhibitor resistance is conferred by the E119V and H275Y mutations, respectively, and adamantane resistance conferred by the S31N mutation.
Genetic and antigenic characterization of influenza A/H5N1 viruses isolated from patients in Indonesia, 2008-2015.
Introduction: The typical drug-resistance substitutions in NA include H275Y, E119D/G, and Q136R for A(H1N1)pdm09; E119V, D151G/V/D, R224K, E276D, R292K, and N294S for A (H3N2); and G104E, E117A/D, H134Y, and R150K for B virus, although additional single and combination mutations may also result in NAI drug resistance (World Health Organization (WHO)).
Functional neuraminidase inhibitor resistance motifs in avian influenza A(H5Nx) viruses.
Discussion: In this study we investigated whether known resistance mutations that occur in human isolated IAV strains (E119V, H274Y, R292K and N294S) function to reduce the susceptibility to NAI drugs in the highly pathogenic H5Nx viruses (H5N2, H5N6 and H5N8) that have been responsible for large scale poultry outbreaks in recent years.
Discussion: Moreover, E119V and H274Y mutations in N8 displayed similar NAI susceptibility profile to the one reported in respective pH1N1 mutants - with E119V showing RI to all three NAIs, and H274Y to OSE and PER.
Discussion: The four mutations: PMID: 32853849
2020
Virology
Abstract: Passage with zanamivir induced an E119G substitution in NA, whereas passage with oseltamivir induced R292K and E119V substitutions that simulated that seen in oseltamivir -treated HPAI H7N9 cases, indicating that the high frequency of resistant strains in the HPAI H7N9 isolates is related to NAIs use.
Influenza A virus hemagglutinin mutations associated with use of neuraminidase inhibitors correlate with decreased inhibition by anti-influenza antibodies.
Highly pathogenic avian influenza H7N9 viruses with reduced susceptibility to neuraminidase inhibitors showed comparable replication capacity to their sensitive counterparts.
Result: However, the substitution E119V in the NA protein induced a mean 90.77-fold increase in the IC50 of oseltamivir (mean IC50 (nM) +
Result: The E119V mutation in N2 has been reported to significantly reduce the sensitivity of the virus to oseltamivir but not to zanamivir.
Result: The nucleotide changes were as follows: for E119V, E/GAA to V/GTA; for A246T, A/GCC to T/ACA; for H274Y, H/CAT to Y/TAT (Table 1).
Figure: Crystal structure model of NA monomer of A/ Anhui1/2013/H7N9 virus (PDB ID: 4MWJ) was used to display and label the four drug resistance mutations (292 K, E119V, A246T or H274Y) by DeepView v4.1.0 software.
IV mutation literature information.
PMID: 
2021
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