Influenza A viruses of swine circulating in the United States during 2009-2014 are susceptible to neuraminidase inhibitors but show lineage-dependent resistance to adamantanes.
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,
Identification of novel compounds against an R294K substitution of influenza A (H7N9) virus using ensemble based drug virtual screening.
PMID: 25589893
2015
International journal of medical sciences
3Introduction: Single amino acid change known as the ""H275Y"" mutation in 2009 H1N1 flu virus and ""R292K"" mutation in influenza A virus is conferred by drug resistance."
Introduction: Orientation and stabilization of various inhibitors in NA protein depend major on two or three Arginine residues in 150 loop, R292K mutation succeeded to unbalance stability and orientation of these inhibitors leading to drug resistance.
Result: The docking results of H7N9 NA agreed well with the experiential results in which NA R292K substitution was highly resistant to Oseltamivir and Peramivir and partially resistant to Zanamivir.
Detection of a transient R292K mutation in influenza A/H3N2 viruses shed for several weeks by an immunocompromised patient.
PMID: 25588658
2015
Journal of clinical microbiology
Abstract: The R292K mutation was identified by direct testing in 3 of 11 respiratory specimens collected throughout the patient's illness but in none of the cultures from those specimens.
Abstract: We describe the case of an immunocompromised patient, positive for influenza A virus (H3N2), in whom the neuraminidase R292K mutation was transiently detected during oseltamivir treatment.
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.
Characterization of drug-resistant influenza A(H7N9) variants isolated from an oseltamivir-treated patient in Taiwan.
PMID: 25124927
2015
The Journal of infectious diseases
Result: Applying the WHO Antiviral Working Group criteria, NA-R292K virus was characterized as exhibiting highly reduced inhibition by oseltamivir and peramivir and reduced inhibition by zanamivir, laninamivir, and A-315675.
Result: In all instances, substitutions occurred at the second nucleotide in the respective triplet: for R292K, AGG AAG; for E119V, GAA GTA; for I222R, ATA AGA; and for I222K, ATA AAA.
Result: In contrast, NA-R292K virus exhibited delayed growth, with infectious titers 2-3 logs lower than those of the other viruses and the highest titer 48 hours after infection.
Result: Inflammatory cell counts (Figure 3B) and total protein concentrations (Figure 3C) in nasal wash specimens
Insight into the oseltamivir resistance R292K mutation in H5N1 influenza virus: a molecular docking and molecular dynamics approach.
PMID: 23794010
2014
Cell biochemistry and biophysics
Abstract: In particular, influenza strains with a R292K NA mutation are highly resistant to the oseltamivir.
Emergence of a novel drug resistant H7N9 influenza virus: evidence based clinical potential of a natural IFN-alpha for infection control and treatment.
PMID: 24350808
2014
Expert review of anti-infective therapy
Abstract: The emerging H7N9 viruses are resistant to the M2-ion channel blockers because of a S31N mutation in the M2 protein; additionally, some H7N9 isolates have gained neuraminidase R292K substitution resulting in broad resistance to neuraminidase inhibitors.
Host immunological response and factors associated with clinical outcome in patients with the novel influenza A H7N9 infection.
PMID: 24350809
2014
Clinical microbiology and infection
Abstract: Genetic characterization of the H7N9 virus revealed an Arg292Lys mutation in the neuraminidase gene associated with oseltamivir-resistance.
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)
An investigational antiviral drug, DAS181, effectively inhibits replication of zoonotic influenza A virus subtype H7N9 and protects mice from lethality.
PMID: 24569063
2014
The Journal of infectious diseases
Method: Because these influenza A(H7N9) isolates contained a mixed viral population, plaque purification was performed in MDCK-SIAT1 cells to separate the oseltamivir-resistant virus variant carrying R292K from the wild-type virus with R292.
Method: Sanger sequencing analyses of the plaque-purified viruses confirmed that R292K was the only amino acid difference between the NAs of wild-type and R292K virus variant.
Method: The HA of the Shanghai/1 R292K variant had a mixture of 151A/S (2013 H7 numbering) and 209G/E, while that of the Taiwan/1 R292K variant showed a D340G substitution, compared with characteristics of the respective wild-type viruses.
IV mutation literature information.
PMID: 
2015
Antiviral research
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