Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells.

作者: I V Chizhmakov , F M Geraghty , D C Ogden , A Hayhurst , M Antoniou

DOI: 10.1113/JPHYSIOL.1996.SP021495

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摘要: 1. The M2 protein of influenza A virus is implicated in transmembrane pH regulation during infection. Whole-cell patch clamp mouse erythroleukaemia cells expressing the surface membrane showed a conductance due to which was specifically blocked by anti-influenza drug rimantadine. 2. ion selectivity rimantadine-sensitive current through determined. Reversal potentials were close equilibrium for gradients and not those Na+, K+ or Cl- concentration gradients. permeability Na+ relative H+ estimated be less than 6 x 10(-7). 3. increased as external decreased below 8.5 approached saturation at an 4, effects attributable driving potential activation low pH. Both permeation could described interaction protons with sites on M2, apparent dissociation constants approximately 0.1 microM 1 microM, respectively, under physiological conditions. 4. can transfer selectively across membranes electrochemical gradient, properties consistent its role modifying virion trans-Golgi

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