A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity

Lawrence H. Pinto*, Gregg R. Dieckmann, Chris S. Gandhi, Carol G. Papworth, Jeffrey Braman, Margaret A. Shaughnessy, James D. Lear, Robert A. Lamb, William F. Degrado

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

304 Scopus citations

Abstract

The M2 protein from influenza A virus forms proton-selective channels that are essential to viral function and are the target of the drug amantadine. Cys scanning was used to generate a series of mutants with successive substitutions in the transmembrane segment of the protein, and the mutants were expressed in Xenopus laevis oocytes. The effect of the mutations on reversal potential, ion currents, and amantadine resistance were measured. Fourier analysis revealed a periodicity consistent with a four-stranded coiled coil or helical bundle. A three-dimensional model of this structure suggests a possible mechanism for the proton selectivity of the M2 channel of influenza virus.

Original languageEnglish (US)
Pages (from-to)11301-11306
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number21
DOIs
StatePublished - Oct 14 1997

ASJC Scopus subject areas

  • General

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