Two research papers in the 08 November 2001 issue of Nature (Vol. 414, No. 6860) investigate the Antrax toxin. The papers have been published online (click on links to access them directly).
Anthrax toxin, secreted by the bacteria Bacillus anthracis, has three parts. One part latches onto a human cell, and injects two more parts that act within the cell. The first paper, from John A. T. Young of the University of Wisconsin-Madison and colleagues, describes the discovery of the receptor on the surface of human cells that the first part of the anthrax toxin (called PA) attaches to, allowing the rest of the toxin to enter. The team find that in vitro a soluble version of this PA receptor mops up the toxin, protecting cells. This research "holds promise for the development of new approaches for the treatment of anthrax," Young’s team conclude.
In the second paper Robert Liddington of The Burnham Institute, La Jolla, California, and colleagues report the structure of another part of the toxin, the anthrax lethal factor (LF). This protein is "critical in the pathogenesis" of the disease. It is an enzyme that inhibits one or more signalling pathways in human cells. The new structural information "can be used in the design of therapeutic agents that would block the activity of LF," say the researchers.
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