Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants

Patrick J. Collins, Lesley F. Haire, Yi Pu Lin, Junfeng Liu, Rupert J. Russell, Philip A. Walker, John J. Skehel, Stephen R. Martin, Alan J. Hay and Steven J. Gamblin ()
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Patrick J. Collins: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Lesley F. Haire: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Yi Pu Lin: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Junfeng Liu: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Rupert J. Russell: Interdisciplinary Centre for Human and Avian Influenza Research, School of Biology, University of St Andrews
Philip A. Walker: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
John J. Skehel: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Stephen R. Martin: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Alan J. Hay: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK
Steven J. Gamblin: MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK

Nature, 2008, vol. 453, issue 7199, 1258-1261

Abstract: Influenza virus: Mechanism of oseltamivir resistance The molecular basis for oseltamivir (Tamiflu) resistance in some clinical isolates of the H5N1 influenza virus has been identified as a mutation in the drug's target, viral neuraminidase. However, the enzyme remains susceptible to zanamivir (Relenza), the other neuraminidase inhibitor in general use. This suggests that public health authorities stockpiling antivirals should augment their supplies of oseltamivir with other antiviral drugs to keep open the options for effective drug-combination treatments.

Date: 2008
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DOI: 10.1038/nature06956

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