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* Department of Physiology and Developmental Biology, Brigham Young University, Provo, Utah; and
Department of Chemistry and Biochemistry, National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida
Correspondence: Address reprint requests to David D. Busath, Dept. of Physiology and Developmental Biology, Brigham Young University, Provo, UT 84602. E-mail: david_busath{at}byu.edu.
Purified M2 protein from the Udorn strain of influenza virus was reconstituted into planar lipid bilayers from liposomes. In 1 mM HCl, the single-channel conductance was measured as 6 pS with open probability of
0.03. The current voltage curve is linear over the achievable voltage range. The current amplitude is amantadine sensitive. In HCl solutions, the single-channel current was essentially invariant with changes in [Cl], [Na+], and [tetraethylammonium] ([TEA+]), but dependent on [H+]. The reversal potential, determined with asymmetrical hydrogen chloride solution, is very close to the equilibrium potential of hydrogen. This appears to be the first report of single-channel proton currents with the full-length M2 protein.
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