Method: Recombinant baculoviruses were generated to express the wild-type, H274Y, H274Y and I222R mutants of NA originating from influenza N1 neuraminidase (NIBRG14 (H5N1)).
Method: The NA structure with I222R and H274Y dual-point mutations was derived using a homology-modeling server.
Method: The assay was conducted in 96-well plates containing active wild-type, H274Y, H274Y and I222R mutants of NA and 100 muM fluorogenic substrate per well in reaction buffer.
Method: The oseltamivir-resistant NA contains a PMID: 29107426
2017
European journal of medicinal chemistry
Abstract: Moreover, 11b showed moderate inhibitions against mutant neuraminidases from H5N1-H274Y and H1N1-H274Y with IC50 values of 2075 nM and 1382 nM, which were inferior to those of oseltamivir carboxylate (6095 nM and 4071 nM).
A Novel Potent and Highly Specific Inhibitor against Influenza Viral N1-N9 Neuraminidases: Insight into Neuraminidase-Inhibitor Interactions.
PMID: 27095056
2016
Journal of medicinal chemistry
Abstract: Like zanamivir, it is highly effective against N1-N9 avian and N1-N2 human viNAs, including H274Y oseltamivir-resistant N1 viNA, due to its C-6 portion still being anchored in the active site, different from the disruption of oseltamivir's C-6 anchoring by H274Y mutation.
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.
H274Y's Effect on Oseltamivir Resistance: What Happens Before the Drug Enters the Binding Site.
PMID: 26703840
2016
Journal of chemical information and modeling
Abstract: However, most of the reported studies on H274Y focused only on the drug-bound system, so the direct effects of the mutation on NA itself prior to drug binding still remain unclear.
Abstract: Increased reports of oseltamivir (OTV)-resistant strains of the influenza virus, such as the H274Y mutation on its neuraminidase (NA), have created some cause for concern.
Abstract: It was observed that the disruption of the NA binding site due to the H274Y mutation was initiated by the repulsive effect of Y274 on the 250-loop, which in turn altered the hydrogen-bonding network around residue 274.
Abstract: Many studies have been conducted in the attempt to uncover the mechanism of OTV resistance in H274Y
Detection of reassortant avian influenza A (H11N9) virus in environmental samples from live poultry markets in China.
PMID: 27268229
2016
Infectious diseases of poverty
Table: H274Y
Sensitive Detection and Simultaneous Discrimination of Influenza A and B Viruses in Nasopharyngeal Swabs in a Single Assay Using Next-Generation Sequencing-Based Diagnostics.
Introduction: Current methods that evaluate antiviral resistance require two independent tests for the S31N substitutions conferring amantadine-resistance and the H274Y substitution conferring oseltamivir-resistance.
Risk of resistant avian influenza A virus in wild waterfowl as a result of environmental release of oseltamivir.
Abstract: In an A(H1N1)/H274Y virus, the OC resistance mutation persisted without selective drug pressure, demonstrating the potential of an IAV with a permissive genetic background to acquire and maintain OC resistance, potentially allowing circulation of the resistant variant among wild birds.
Introduction: However, since 2010/2011, an increasing number of community cases with OC-resistant A(H1N1)/pdm09 viruses have been reported without previous oseltamivir exposure; in nearly all instances the resistance has been conferred by the H274Y substitution in NA.
Introduction: In IAVs containing N1 NA proteins the most common resistance-related change seen in vivo is the framework substitution H274Y (N2 numbering, used hereafter), whereas in N2-containing viruses the framework E119V
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
Human Monoclonal Antibody 81.39a Effectively Neutralizes Emerging Influenza A Viruses of Group 1 and 2 Hemagglutinins.
IV mutation literature information.
PMID: 
2017
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