Abstract
The recent outbreaks of avian flu in Southeast Asia and swine flu in Mexico City painfully exemplify the ability of the influenza virus to rapidly mutate and develop resistance to modern medicines. This review seeks to detail the molecular mechanism by which the influenza virus has obtained resistance to amino-adamantyls, one of only two classes of drugs that combat the flu. Amino-adamantyls target the viral M2 H(+) channel and have become largely ineffective due to mutations in the transmembrane domain of the protein. Herein we describe these resistance rendering mutations and the compounded effects they have upon the protein's function and resulting virus viability.
2010 Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adamantane / pharmacology*
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Amantadine / pharmacology
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Amino Acid Sequence
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Drug Resistance, Viral / genetics
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Genes, Viral
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Hemagglutinin Glycoproteins, Influenza Virus / chemistry
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Hemagglutinin Glycoproteins, Influenza Virus / drug effects
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Hemagglutinin Glycoproteins, Influenza Virus / genetics
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Humans
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Influenza A virus / chemistry
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Influenza A virus / drug effects
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Influenza A virus / genetics
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Influenza A virus / pathogenicity
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Influenza, Human / drug therapy*
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Influenza, Human / virology
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Ion Channels / chemistry
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Ion Channels / drug effects
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Ion Channels / genetics
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Protein Stability
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Protein Structure, Tertiary
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Rimantadine / pharmacology
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Sequence Homology, Amino Acid
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Viral Matrix Proteins / chemistry
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Viral Matrix Proteins / drug effects
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Viral Matrix Proteins / genetics
Substances
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Hemagglutinin Glycoproteins, Influenza Virus
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Ion Channels
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M2 protein, Influenza A virus
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Viral Matrix Proteins
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Rimantadine
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Amantadine
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Adamantane