Abstract: Consequently, a cost-effective oligonucleotide microarray visualization method, which was based on quantum dot-catalyzed silver deposition, was developed and evaluated for the simultaneous detection of neuraminidase H275Y and E119V; matrix protein 2 V27A and S31N mutations of influenza A (H3N2), seasonal influenza A (H1N1), and 2009 influenza A (H1N1).
Introduction: Furthermore, more than 99% of amantadine resistance generally resulted from mutations V27A and S31N in M2.
Introduction: The objective of this study was to design a cost-effective oligonucleotide microarray visualization method to simultaneously detect NA&n
Genetic diversity of early (1998) and recent (2010) avian influenza H9N2 virus strains isolated from poultry in Iran.
Abstract: An analysis of the viral amino acid sequence of the M2 protein of the recent strain revealed a V27A mutation, which is associated with amantadine resistance in avian influenza virus.
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
Abstract: Inhibition of the wild-type (WT) M2 channel and the amantadine-resistant A/M2-S31N and A/M2-V27A mutant ion channels were measured in Xenopus oocytes using two-electrode voltage clamp (TEV) assays.
Abstract: Of note, several compounds inhibited the A/M2 V27A mutant ion channel, one of them with submicromolar IC50.
Abstract: The antiviral activity of three novel dual WT and A/M2-V27A channels inhibitors was confirmed by influenza virus yield assays.
Introduction: Alkylation of 14a to 15a reduced the inhibitory potency both for the wt and the V27A mutant.
Introduction: Also, since recent MD calculations sugg
Exploring organosilane amines as potent inhibitors and structural probes of influenza a virus M2 proton channel.
PMID: 21819109
2011
Journal of the American Chemical Society
Abstract: Organosilane amine inhibitors were found to be generally as potent as their carbon analogues in targeting WT A/M2 and more potent against the drug-resistant A/M2-V27A mutant.
Introduction: 4,4-Dimethyl silacyclohexane amines 10 and 14 showed a high potency against the WT A/M2 and only minimal inhibition against A/M2-V27A mutant (Table 2), which was expected, as A/M2-V27A prefers binding molecules with extended conformations.
Introduction: A/M2 is more conserved than other drug targets of influenza A virus with only three predominant drug resistant mutations S31N, V27A and
Molecular dynamics simulation directed rational design of inhibitors targeting drug-resistant mutants of influenza A virus M2.
PMID: 21744829
2011
Journal of the American Chemical Society
Abstract: Among these mutations, the V27A mutation was prevalent among transmissible viruses under drug selection pressure.
Abstract: However, most of the current virulent influenza A viruses carry drug-resistant mutations alongside the drug binding site, such as S31N, V27A, and L26F, etc., each of which might be dominant in a given flu season.
Abstract: Until now, V27A has not been successfully targeted by small molecule inhibitors, despite years of extensive medicinal chemistry research efforts and high throughput screening.
Introduction: Although a variety of mutations can lead to amantadine-resistance in vitro, only three mutants, S31N, V27A and L26F, are generally observed in transmissible viruses
Exploring the size limit of templates for inhibitors of the M2 ion channel of influenza A virus.
PMID: 21466220
2011
Journal of medicinal chemistry
Abstract: Inhibition of the wild-type (wt) M2 channel and the A/M2-S31N and A/M2-V27A mutant ion channels were measured in Xenopus oocytes using two-electrode voltage clamp (TEV) assays.
Introduction: Also, at 100 muM, 8 inhibited the A/M2 V27A channel activity by 10.6%, quite similar to Amt (10.8%).
Introduction: Interestingly, 24 (at a concentration of 100 muM) inhibited the A/M2 V27A
Method: A/M2 S31N and A/M2 V27A mutants were generated by QuikChange site-directed mutagenesis kit (Agilent Technologies).
Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.
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.
Result: Now we see that V27S binds amantadine while V27A does not.
Solution NMR structure of the V27A drug resistant mutant of influenza A M2 channel.
PMID: 20833142
2010
Biochemical and biophysical research communications
Method: Structure determination of the V27A mutant.
Method: The M218-60 structure was obtained by refining a homology model derived from the WT18-60 structure against V27A NMR restraints (including 948 intra- and 60 inter-subunit NOE-derived distance restraints).
Method: The structure of the V27A amantadine-resistant mutant has been deposited to the Protein Data Bank with PDB accession code 2KWX.
Result: A comparison of the pores of the WT, V27A, and S31N structures (Figure 3) show that the overall architectures of the pores are similar among the three variants except for local changes around the mutated residues.
Result: An obvious difference in the V27A structure is that the channel entrance is much wider than in WT.
Result: Another interesting detail
Coexistence of two adamantane binding sites in the influenza A M2 ion channel.
Abstract: Furthermore, by examining drug binding to M2 mutant constructs (V27A, S31N, and D44A), it was possible to probe the location of the two binding sites.
In vitro system for modeling influenza A virus resistance under drug pressure.
PMID: 20498316
2010
Antimicrobial agents and chemotherapy
Abstract: Sequencing of the M2 gene revealed that mutations appeared at between 48 and 72 h of drug treatment and that the mutations were identical to those identified in the clinic for amantadine-resistant viruses (e.g., V27A, A30T, and S31N).
IV mutation literature information.
PMID: 
2013
PloS one
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