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Science 330 (6003): 456-458

Copyright © 2010 by the American Association for the Advancement of Science

Structural Biology

The Flu's Proton Escort

Giacomo Fiorin,1 Vincenzo Carnevale,1 William F. DeGrado2

The influenza A virus, which causes seasonal flu, poses a major threat to human health. One recent focus of research has been the M2 protein, a small membrane protein that enables hydrogen ions to enter the viral particle (1, 2); this "proton channel" plays a critical role in enabling the virus to infect cells and replicate and in other processes (3, 4). In recent flu seasons, a mutation in the M2 protein has rendered the virus resistant to two common antiviral drugs, amantadine and rimantadine. Efforts to develop new antiviral drugs would benefit from a better understanding of M2's structure and how drugs act on the protein, but recent studies have often produced conflicting results. This trend continues with two papers in this issue, by Sharma et al. (5) on page 509, and Hu et al. (6) on page 505. There are, however, possible explanations for the apparent inconsistencies in these and other recently reported structures (7, 8).

1 Institute for Computational Molecular Science and Department of Chemistry, Temple University, Philadelphia, PA 19122-6078, USA.
2 Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.

E-mail: wdegrado{at}

Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.
A. Ghosh, J. Qiu, W. F. DeGrado, and R. M. Hochstrasser (2011)
PNAS 108, 6115-6120
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