Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block
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- C Wang
- Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500.
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- K Takeuchi
- Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500.
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- L H Pinto
- Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500.
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- R A Lamb
- Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208-3500.
書誌事項
- 公開日
- 1993-09
- 権利情報
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 10.1128/jvi.67.9.5585-5594.1993
- 公開者
- American Society for Microbiology
この論文をさがす
説明
<jats:p>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 Kis for amantadine block.</jats:p>
収録刊行物
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- Journal of Virology
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Journal of Virology 67 (9), 5585-5594, 1993-09
American Society for Microbiology