Amid heightened concern over a possible epidemic of bird flu in humans, scientists in the United States and Taiwan are reporting critical new insights into the architecture of a key enzyme in the H5N1 avian influenza virus that enables the virus to spread.
Rommie E. Amaro and colleagues focused on what has been termed the "hot pocket," or more technically "the 150-loop." This chain of amino acids forms a cavity in the neuraminidase enzyme that facilitates H5N1's spread. Anti-flu drugs called neuraminidase inhibitors work by entering and binding to the hot pocket, almost like a hand fitting into a glove.
In the new study, researchers report that the hot pocket actually can have internal shapes substantially different than previously believed. That new structural understanding of the 150-loop could be valuable in efforts to design new and more effective anti-flu drugs, they state. Drugs capable of fitting more snugly into the cavity could yield a class of neuraminidase inhibitors that are more effective against H5N1-like flu viruses.
The report is scheduled for the June 20 issue of the Journal of the American Chemical Society. The title of the article is "Remarkable Loop Flexibility in Avian Influenza N1 and Its Implications for Antiviral Drug Design."
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