Influenza virus M2 protein has ion channel activity

Cell. 1992 May 1;69(3):517-28. doi: 10.1016/0092-8674(92)90452-i.


The influenza virus M2 protein was expressed in Xenopus laevis oocytes and shown to have an associated ion channel activity selective for monovalent ions. The anti-influenza virus drug amantadine hydrochloride significantly attenuated the inward current induced by hyperpolarization of oocyte membranes. Mutations in the M2 membrane-spanning domain that confer viral resistance to amantadine produced currents that were resistant to the drug. Analysis of the currents of these altered M2 proteins suggests that the channel pore is formed by the transmembrane domain of the M2 protein. The wild-type M2 channel was found to be regulated by pH. The wild-type M2 ion channel activity is proposed to have a pivotal role in the biology of influenza virus infection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amantadine / pharmacology
  • Amino Acid Sequence
  • Animals
  • Electric Conductivity / drug effects
  • Hydrogen-Ion Concentration
  • Ion Channels / drug effects
  • Ion Channels / physiology*
  • Membrane Potentials
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Orthomyxoviridae / physiology*
  • Viral Envelope Proteins / physiology*
  • Viral Matrix Proteins / physiology*
  • Xenopus laevis


  • Ion Channels
  • M-protein, influenza virus
  • M2 protein, Influenza A virus
  • Viral Envelope Proteins
  • Viral Matrix Proteins
  • Amantadine