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- W2025428445 abstract "The integral matrix protein M2 of influenza A virus forms a pH-gated proton channel in the viral lipid envelope upon infecting host cells. The conductance of protons through the M2 channels in the low-pH endosomes (pH < 5.0)[1] acidifies the viral interior and facilitates the dissociation of the viral genome from the matrix protein M1. Although X-ray crystallography[2] and NMR[3] studies using truncated proteins concluded that M2 stably forms a tetrameric channel that opens at acidic pH, the oligomeric state of the full length protein on biomembranes is not clear yet. In the present study, we examined the oligomeric state of the full length M2 protein on the plasma membrane of living cells by using fluorescence resonance energy transfer (FRET) among the M2 proteins labeled with fluorophores by the coiled-coil method[4]. Contrary to previous models, M2 formed dimers at neutral pH and the dimers were converted to tetramers at pH 4.9. The tetramerization and channel activity were completely inhibited in the presence of the antiviral Amantadine hydrochloride (Am) at low pH. In contrast, the S31N mutant resistant to Am formed dimers independent of pH and the presence of Am, and the channel activity was not blocked by Am. These results indicate that the resistance of the S31N mutant could be attributed to its ability to conduct protons as dimers without forming tetramers.References[1] J. Chem. Biol. (2010) 189; 1171[2] Nature (2008) 451; 596[3] Nature (2008) 451; 591[4] ACS, Chem. Biol. (2008) 3; 341" @default.
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- W2025428445 date "2013-01-01" @default.
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- W2025428445 title "Oligomeric States of Full Length Influenza a Virus M2 Proteins on Biological Membranes" @default.
- W2025428445 doi "https://doi.org/10.1016/j.bpj.2012.11.1554" @default.
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