Researchers at Rice University and the University of Texas at Austin (UT) have investigated the structure of the long flexible tail of the influenza virus' nucleoprotein. This tail is present in all strains of influenza A including lethal bird flu, Hong Kong flu, and Spanish flu. "There is a small binding pocket for the tail loop of the protein that appears to be a promising target for a new class of antiviral drugs," explains team leader Jane Tao who is working with UT's Robert Krug, "We know from previous genetic studies that this tail loop is almost identical across strains of influenza A, so drugs that target the tail have a high potential of being effective against multiple strains, including the H5N1 [bird flu] strains." The team has found that even seemingly minor changes to the protein tail prevent it from fulfilling a key role in viral replication - linking together to form structural columns used by the virus to transmit copies of itself. New antiviral drugs that circumvent viral resistance are desperately needed if we are to ward off a flu pandemic.
The long tail of bird flu