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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Computer Simulation
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Cysteine
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Electric Conductivity
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Female
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Influenza A virus / physiology*
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Ion Channels / chemistry
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Ion Channels / physiology
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oocytes / physiology
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Protein Conformation*
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Substrate Specificity
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Viral Matrix Proteins / chemistry*
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Viral Matrix Proteins / physiology*
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Xenopus laevis
Substances
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Ion Channels
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M-protein, influenza virus
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M2 protein, Influenza A virus
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Recombinant Proteins
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Viral Matrix Proteins
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Cysteine