Resistance to neuraminidase inhibitors conferred by an R292K mutation in a human influenza virus H7N9 isolate can be masked by a mixed R/K viral population.
Abstract: IMPORTANCE: The neuraminidase (NA) inhibitors oseltamivir and zanamivir are currently the front-line therapeutic options against the novel H7N9 influenza viruses, which possess an S31N mutation that confers resistance to the M2 ion channel blockers.
Introduction: Neuraminidase (NA) inhibitors have been used as the front-line therapeutic option because the novel H7N9 viruses contain the S31N mutation in the M2 protein conferring resistance to the M2 ion channel blockers.
3-Azatetracyclo[5.2.1.1(5,8).0(1,5)]undecane derivatives: from wild-type inhibitors of the M2 ion channel of influenza A virus to derivatives with potent activity against the V27A mutant.
PMID: 24237039
2013
Journal of medicinal chemistry
Introduction: L26F, V27A, and S31N) have been observed in transmissible viruses, with the S31N mutation being the most frequently occurring Am
Introduction: In agreement with the TEV assays (see above), all the compounds were not active against the amantadine-resistant A/PR/8/34 strain that carries the M2-S31N mutation.
Introduction: In our basic CPE reduction assays with influenza virus, performed in MDCK cell cultures, three virus strains were used: the A/PR/8/34 strain, an A/H1N1 virus with two amantadine-resistance mutations (S31N and V27T) in the A/M2 protein; the A/HK/7/87 strain, which has a wt A/M2 protein, and the B/HK/5/72 strain.
Treatment of oseltamivir-resistant influenza A (H1N1) virus infections in mice with antiviral agents.
Discussion: Resistance of the pandemic 2009 H1N1 viruses to adamantanes has been previously described, and is attributable to an S31N mutation in the M2 gene.
Design and synthesis of pinanamine derivatives as anti-influenza A M2 ion channel inhibitors.
Abstract: Several imidazole and guanazole derivatives of pinanamine were found to inhibit WT A/M2 to a comparable degree as amantadine and one of these compounds 12 exhibits weak inhibition of A/M2-S31N mutant and it is marginally more effective in inhibiting S31NM2 than amantadine.
Molecular characterization of avian-like H1N1 swine influenza a viruses isolated in Eastern China, 2011.
Abstract: The M2 proteins of the isolates have the mutation (S31N), a characteristic marker of the European avian-like swine viruses since about 1987, which may confer resistance to amantadine and rimantadine antivirals.
Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.
Introduction: The drugs, amantadine and rimantadine, were effective against influenza A until recently when the influenza A strains became dominated by an S31N mutation displaying drug resistance.
Result: <
Result: 6 shows that the PISEMA spectra of 5 15N-labeled leucine residues in the M2 TM domain do not change significantly in the presence (red) or absence (black) of amantadine for the S31N, V27A, and A30T mutants.
Result: In order to further investigate the binding site of amantadine in M2 channels, we prepared mutants of the AM2 TM domain corresponding to the naturally occurring drug-resistant mutations, V27S, V27A, A30T, and S31N.
Oseltamivir-resistant influenza A and B viruses pre- and postantiviral therapy in children and young adults with cancer.
PMID: 21048522
2011
The Pediatric infectious disease journal
Introduction: Resistance to the second class of anti-influenza drugs, adamantanes, results in most cases from a single serine to asparagine amino acid replacement (S31N) in the matrix M2 protein, which can interfere with the drug's ability to block M2 ion channel activity and viral replication.
Result: Susceptibility to adamantanes was tested for all oseltamivir-resistant influenza A (H3N2) viruses by sequence analysis of the M gene; all strains had an S31N mutation in the transmembrane region of the M2 protein and were therefore resistant to these drugs (data not shown).
Genotypic and phenotypic resistance of pandemic A/H1N1 influenza viruses circulating in Germany.
Abstract: In addition, analysis of 1011 pandemic A/H1N1 virus samples by a PSQ-based assay according to the WHO protocol revealed the presence of mutation S31N in the M2 protein that conferred resistance to M2 ion channel inhibitors.
Pandemic H1N1 2009 influenza virus with the H275Y oseltamivir resistance neuraminidase mutation shows a small compromise in enzyme activity and viral fitness.
PMID: 21172786
2011
The Journal of antimicrobial chemotherapy
Introduction: Pandemic influenza A/H1N1 2009 virus (pH1N1) crossed into humans carrying a well-characterized amantadine-resistance mutation, S31N, within the M2 ion channel protein, rendering the adamantane class of antiviral drug ineffective against the virus.
Nationwide molecular surveillance of pandemic H1N1 influenza A virus genomes: Canada, 2009.
IV mutation literature information.
PMID: 
2013
mBio
Browser Board
Co-occurred Entities
Filtrator
ViMRT