Editor's Summary
31 January 2008
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.
News and Views: Ion channels: Coughing up flu's proton channels
Two research teams have captured snapshots of the influenza virus's membrane-bound hydrogen-ion channel, which is essential for infection and virulence. Their findings agree on the basics, but differ in details.
Christopher Miller
doi:10.1038/451532a
Letter: Structure and mechanism of the M2 proton channel of influenza A virus
Jason R. Schnell & James J. Chou
doi:10.1038/nature06531
First paragraph | Full Text | PDF (716K) | Supplementary information
Letter: 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 & William F. DeGrado
doi:10.1038/nature06528
First paragraph | Full Text | PDF (689K) | Supplementary information
