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Joan Stephenson, PhD

JAMA. 2006;296:1345.

	Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings.

Researchers from the National Institute for Medical Research in London have discovered a structural element in a key enzyme of the H5N1 avian influenza virus that presents a new avenue for designing anti-influenza drugs (Russell RJ et al. Nature. doi:10.1038/nature05114 [published online ahead of print August 16, 2006]).

The enzyme, neuraminidase, has 9 subtypes, and design of the anti-flu drugs oseltamivir and zanamivir was based on the N2 and N9 forms of the virus. In the current work, the researchers used x-ray crystallography to examine the N1 subtype found in H5N1 avian influenza, as well as 2 other forms (N4 and N8). They found that when N1, N4, or N8 bind their normal target, a small cavity close to the active site opens up.

"One could design a chemical group with the right shape, size and electronic charge to fit snugly into the newly discovered cavity," . . . [Full Text of this Article]

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