Newly discovered protein kills anthrax bacteria by exploding their ...( Not all biological weapons are created ...)

Not all biological weapons are created equal. They are separated into categories A through C, category A biological agents being the scariest: They are easy to spread, kill effectively and call for special actions by the pubic health system. One of these worrisome organisms is anthrax, which has already received its fair share of media attention. But work in Vince Fischetti's laboratory at Rockefeller University suggests that a newly discovered protein could be used to fight anthrax infections and even decontaminate areas in which anthrax spores have been released.

"Anthrax is the most efficient biowarfare agent. Its spores are stable and easy to produce, and once someone inhales them, there is only a 48-hour window when antibiotics can be used," says Fischetti. "We've found a new protein that could both potentially expand that treatment window and be used as a large-scale decontaminant of anthrax spores." Because anthrax spores are resistant to most of the chemicals that emergency workers rely on to sterilize contaminated areas, a solution based on the protein would be a powerful tool for cleaning up after an anthrax attack.

All bacteria, anthrax included, have natural predators called bacteriophage. Just as viruses infect people, bacteriophage infect bacteria, reproduce, and then kill their host cell by bursting out to find their next target. The bacteriophage use special proteins, called lysins, to bore holes in the bacteria, causing them to literally explode. Fischetti and colleagues identified one of these lysins, called PlyG, in 2004, and showed that it could be used to help treat animals and humans infected by anthrax. Now, they have identified a second lysin, which they have named PlyPH, with special properties that make it not only a good therapeutic agent, but also useful for large-scale decontamination of areas like buildings and military equipment.

The new protein has several advantages. Most lysins, including PlyG, are only activ
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Contact: Kristine Kelly
kkelly@rockefeller.edu
212-327-7146
Rockefeller University
21-Apr-2006

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