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New finding points way to foiling anthrax's tricks

dents Rebecca J. Abergel and Trisha M. Hoette approached an anthrax research laboratory run by B. Rowe Byers, professor of microbiology at the University of Mississippi Medical Center, to obtain samples of anthrax siderophores. Because bacteria secrete siderophores, these molecules can be separated from the bacteria and studied without danger of infection.

Using these anthrax bacteria extracts, Abergel and Hoette isolated the two siderophores, bacillibactin and petrobactin, and showed that siderocalin tightly binds bacillibactin, preventing it from capturing iron from human cells. However, siderocalin does not prevent petrobactin from binding iron.

Interestingly, bacillibactin is very similar to siderophores in other bacteria, including enterobactin, which is produced by several pathogenic bacteria that live in the gut, such as Salmonella enterica and pathogenic strains of E. coli. These two bacteria also contain a second siderophore, aerobactin, with a molecular structure similar to petrobactin.

The researchers suggest that producing a second, stealth siderophore - petrobactin or aerobactin - that has a different molecular structure than bacillibactin and enterobactin may be a common response by bacteria to the human body's production of siderocalin.

The research could lead to anti-anthrax drugs that target petrobactin synthesis or iron-uptake, or to anthrax sensors that detect petrobactin, which is not known to occur in any other pathogenic bacteria.
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Source:University of California - Berkeley


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