The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design

Rupert J. Russell, Lesley F. Haire, David J. Stevens, Patrick J. Collins, Yi Pu Lin, G. Michael Blackburn, Alan J. Hay, Steven J. Gamblin and John J. Skehel ()
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Rupert J. Russell: MRC National Institute for Medical Research, The Ridgeway
Lesley F. Haire: MRC National Institute for Medical Research, The Ridgeway
David J. Stevens: MRC National Institute for Medical Research, The Ridgeway
Patrick J. Collins: MRC National Institute for Medical Research, The Ridgeway
Yi Pu Lin: MRC National Institute for Medical Research, The Ridgeway
G. Michael Blackburn: University of Sheffield
Alan J. Hay: MRC National Institute for Medical Research, The Ridgeway
Steven J. Gamblin: MRC National Institute for Medical Research, The Ridgeway
John J. Skehel: MRC National Institute for Medical Research, The Ridgeway

Nature, 2006, vol. 443, issue 7107, 45-49

Abstract: Abstract The worldwide spread of H5N1 avian influenza has raised concerns that this virus might acquire the ability to pass readily among humans and cause a pandemic. Two anti-influenza drugs currently being used to treat infected patients are oseltamivir (Tamiflu) and zanamivir (Relenza), both of which target the neuraminidase enzyme of the virus. Reports of the emergence of drug resistance make the development of new anti-influenza molecules a priority. Neuraminidases from influenza type A viruses form two genetically distinct groups: group-1 contains the N1 neuraminidase of the H5N1 avian virus and group-2 contains the N2 and N9 enzymes used for the structure-based design of current drugs. Here we show by X-ray crystallography that these two groups are structurally distinct. Group-1 neuraminidases contain a cavity adjacent to their active sites that closes on ligand binding. Our analysis suggests that it may be possible to exploit the size and location of the group-1 cavity to develop new anti-influenza drugs.

Date: 2006
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DOI: 10.1038/nature05114

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