Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block

C. Wang, K. Takeuchi, L. H. Pinto, R. A. Lamb*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

403 Scopus citations


The influenza A virus M2 integral membrane protein has ion channel activity which can be blocked by the antiviral drug amantadine. The M2 protein transmembrane domain is highly conserved in amino acid sequence for all the human, swine, equine, and avian strains of influenza A virus, and thus, known amino acid differences could lead to altered properties of the M2 ion channel. We have expressed in oocytes of Xenopus laevis the M2 protein of human influenza virus A/Udorn/72 and the avian virus A/chicken/Germany/34 (fowl plague virus, Rostock) and derivatives of the Rostock ion channel altered in the presumed pore region. The pH of activation of the M2 ion channels and amantadine block of the M2 ion channels were investigated. The channels were found to be activated by pH in a similar manner but differed in their apparent K(i)s for amantadine block.

Original languageEnglish (US)
Pages (from-to)5585-5594
Number of pages10
JournalJournal of virology
Issue number9
StatePublished - 1993

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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