Structure and mechanism of the M2 proton channel of influenza A virus

Jason R. Schnell and James J. Chou ()
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Jason R. Schnell: Harvard Medical School, Boston, Massachusetts 02115, USA
James J. Chou: Harvard Medical School, Boston, Massachusetts 02115, USA

Nature, 2008, vol. 451, issue 7178, 591-595

Abstract: Influenza changes channels Until recently, the pH-gated proton channel of influenza A virus, M2, was effectively targeted by amantadine-based antivirals, but resistance to these drugs is now widespread. Two groups now present structural studies of M2 proton channel. Jason Schnell and James Chou determine the structure of a 38-residue segment of M2, in complex with rimantadine, by NMR spectroscopy. Amanda Stouffer et al. determined the crystal structure of a 25-residue fragment of M2, with and without amantadine, using X-ray diffraction. Strikingly, the resulting structures suggest two very different mechanisms by which the drug inhibits the channel. The proposed mechanisms are discussed by Christopher Miller in an accompanying News & Views article.

Date: 2008
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DOI: 10.1038/nature06531

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