Scientists from U.S. Army Medical Research Institute of Infectious Diseases and Brookhaven National Laboratory have taken the first step toward designing an effective antidote to the most potent form of the botulinum neurotoxin, according to an announcement by Brookhaven on Tuesday.
The research team have found that they can trick the toxin to bypass its normal binding protein, thereby blocking its deadly action. The results of their research are published in the latest online issue of the Journal of Biological Chemistry.
"We have found a highly efficient inhibitor of botulinum neurotoxin type A -- the most potent of seven neurotoxins produced by the bacterium Clostridium botulinum. This finding can lead to a very effective drug to stop the devastating effects of the toxin," said Brookhaven Lab biologist Subramanyam Swaminathan. "We intend to do further research to tailor the inhibitor for the best results."
Botulinum neurotoxin is responsible for the deadly food poisoning disease botulism and for the beneficial effects of smoothing out facial wrinkles. However, it can also be used as a dreaded biological weapon. When ingested or inhaled, less than a billionth of an ounce can cause muscle paralysis and eventual death.
Although experimental vaccines administered prior to exposure can inhibit the destructive action of this neurotoxin -- the most deadly protein known to humans -- no effective pharmacological treatment exists.
To block the toxin's action, the researchers designed four "decoy" protein fragments that mimic the structure of the protein to which the toxin ordinarily binds. The toxin then attaches itself to the decoy fragments instead of to the cell's protein. This re-routing of the toxin allows neurotransmitters to keep functioning, thus stopping the toxin's pathological effects.
The scientists used x-ray techniques to see how the toxin binds to the protein inhibitors. They found that all four decoy proteins are efficient at inhibiting the toxin's binding to the cell's protein, but one of them in particular is by far the best of any known inhibitors. The scientists' next step in this process is to transform the most effective of the four protein fragments into a drug-like molecule before clinical testing is done.
Source: Xinhua
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