Structural basis for the function and inhibition of an influenza virus proton channel

Amanda L. Stouffer, Rudresh Acharya, David Salom, Anna S. Levine, Luigi Di Costanzo, Cinque S. Soto, Valentina Tereshko, Vikas Nanda, Steven Stayrook and William F. DeGrado ()
Additional contact information
Amanda L. Stouffer: School of Medicine
Rudresh Acharya: School of Medicine
David Salom: School of Medicine
Anna S. Levine: School of Medicine
Luigi Di Costanzo: University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Cinque S. Soto: School of Medicine
Valentina Tereshko: University of Chicago, Chicago, Illinois 60637, USA
Vikas Nanda: School of Medicine
Steven Stayrook: School of Medicine
William F. DeGrado: School of Medicine

Nature, 2008, vol. 451, issue 7178, 596-599

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/nature06528

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