pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

Results indicate that M2 proton channel tetramerization and amantadine binding to the protein occurs preferentially at higher pH with the involvement of histidine amino acid residue. Data suggest that the drug competes with protons for binding to the deprotonated tetramer protein of the influenza A virus.