Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data.
The M2 proton channel from influenza A virus forms proton-selective ion channels, which are the target of the drug amantadine. Here, existing experimental data are quantitatively examined for insights into mechanisms to account for the pH- and voltage-dependences of M2 proton conduction. The analysis shows that a model involving protonation equilibria of His37, including pH-dependent changes in the relative rates of diffusion on either side of the pore, is quantitatively able to account for recently reported electrophysiological data examining the pH- and voltage-dependences of Rostock and Weybridge strain M2 proton conduction.
Lear
James D
JD
Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine of the University of Pennsylvania, Philadelphia, PA 19104-6059, USA. lear@mail.med.upenn.edu
D000465:Algorithms; D000547:Amantadine / Q000494:pharmacology; D000818:Animals; D004594:Electrophysiology; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007477:Ions; D007700:Kinetics; D051379:Mice; D008962:Models, Theoretical; D011522:Protons; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000502:physiology*; D000086082:Viroporin Proteins
D000547:Amantadine; D006639:Histidine; D007477:Ions; D011522:Protons; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins