IV mutation literature information.


  Mutation analysis of 2009 pandemic influenza A(H1N1) viruses collected in Japan during the peak phase of the pandemic.
 PMID: 21572517       2011       PloS one
Discussion: Among these NA substitutions, a His-to-Tyr (H274Y) substitution at position 274 is one of the best characterized oseltamivir-resistance markers.


  Dynamic residue interaction network analysis of the oseltamivir binding site of N1 neuraminidase and its H274Y mutation site conferring drug resistance in influenza A virus.
 PMID: 21628810       2011       Journal of infection in developing countries
Abstract: INTRODUCTION: We investigated the frequency of H274Y-positive swine-origin 2009 A (H1N1) influenza virus outbreak in Thailand during May-August 2009.METHODOLOGY: This study sought to find Oseltamivir resistance mutation H274Y by using pyrosequencing.
Abstract: RESULTS: From 8,710 real-time RT-PCR swine-origin 2009 A(H1N1) influenza virus-positive specimens, 100 randomly selected samples identified one such virus with H274Y mutationusing pyrosequencing.


  Neuraminidase inhibitor R-125489--a promising drug for treating influenza virus: steered molecular dynamics approach.
 PMID: 21693105       2011       Biochemical and biophysical research communications
Abstract: Based on results obtained by SMD and the molecular mechanics-Poisson-Boltzmann surface area method, we predict that R-125489 can be used to treat not only wild-type but also tamiflu-resistant N294S, H274Y variants of A/H5N1 virus as its binding affinity does not vary much across these systems.


  Study of Tamiflu sensitivity to variants of A/H5N1 virus using different force fields.
 PMID: 21834591       2011       Journal of chemical information and modeling
Abstract: GROMOS96 43a1 provides a lower correlation as it supports Oseltamivir to be more resistant to N294S than H274Y.
Abstract: In this paper, we consider the impact of four main force fields, AMBER99SB, CHARMM27, GROMOS96 43a1, and OPLS-AA/L, on the binding affinity of Oseltamivir carboxylate to the wild-type and Y252H, N294S, and H274Y mutants of glycoprotein neuraminidase from the pandemic A/H5N1 virus.
Abstract: They correctly capture the binding ranking Y252H WT N294S H274Y observed in experiments (Collins, P.


  Role of permissive neuraminidase mutations in influenza A/Brisbane/59/2007-like (H1N1) viruses.
 PMID: 22174688       2011       PLoS pathogens
Introduction: The H275Y (H274Y in N2 numbering) NA mutation conferring resistance to oseltamivir and peramivir has been detected with increasing frequency in seasonal A/H1N1 viruses since 2007 to the extent that almost all characterized A/Brisbane/59/2007-like (Bris07) (H1N1) influenza strains that circulated worldwide during the 2008-09 season were H275Y variants.


  [Oseltamivir resistance depends on the position 273 amino acid of neuraminidase of the type A influenza virus (H1N1), circulating in human population].
 PMID: 22332369       2011       Bioorganicheskaia khimiia
Abstract: Phenylalanine at position 273 in neuraminidase indicates a higher propensity to influenza virus mutation H274Y, leading to the appearance of resistant strains.


  Evaluation of a rapid molecular algorithm for detection of pandemic influenza A (H1N1) 2009 virus and screening for a key oseltamivir resistance (H275Y) substitution in neuraminidase.
 PMID: 19857993       2010       Journal of clinical virology
Table: H274Y


  Host cell selection of influenza neuraminidase variants: implications for drug resistance monitoring in A(H1N1) viruses.
 PMID: 19917319       2010       Antiviral research
Abstract: Mutations at D151 without H274Y, did not elevate IC(50) for any tested NAI, however, Q136K alone significantly reduced susceptibility to zanamivir (36-fold), peramivir (80-fold) and A-315675 (114-fold) but not oseltamivir.
Abstract: Pyrosequencing analysis confirmed H274Y mutation (H275Y in N1 numbering) in the neuraminidase (NA) gene of oseltamivir-resistant viruses.
Abstract: Viruses with very high IC(50) for oseltamivir and peramivir, and elevated IC(50) for zanamivir, had H274Y in addition to mutations at D151 and/or Q136, residues which can potentially confer NAI resistance based on recent N1 NA crystal structure dat


  Dynamic residue interaction network analysis of the oseltamivir binding site of N1 neuraminidase and its H274Y mutation site conferring drug resistance in influenza A virus.
 PMID: 19962344       2010       Journal of clinical virology
Abstract: CONCLUSIONS: A dramatic surge in oseltamivir-resistant A(H1N1) viruses possessing the NA-H274Y substitution was detected in Japan during the 2008-2009 season.
Abstract: Oseltamivir resistance was determined by an H274Y-specific real-time PCR cycling probe assay and a neuraminidase inhibition assay.
Abstract: RESULTS: Three of 687 (0.4%) A(H1N1) viruses from the 2007-2008 season and 745 of 745 (100%) viruses from the 2008-2009 season carried the NA-H274Y substitution and demonstrated a >300-fold reduction in oseltamivir susceptibility.


  Laninamivir prodrug CS-8958, a long-acting neuraminidase inhibitor, shows superior anti-influenza virus activity after a single administration.
 PMID: 20047917       2010       Antimicrobial agents and chemotherapy
Abstract: CS-8958 also significantly reduced the titers of an oseltamivir-resistant H1N1 virus with a neuraminidase H274Y substitution in a mouse infection model.



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