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Botulism study could lead to new vaccines and treatments to counter bioterrorist attacks

o its specific protein receptor on the surface of a neuron.

The scientists discovered that the neurotoxin works by taking advantage of the neuronal signaling system in which tiny protein-lipid sacs (synaptic vesicles) carry chemical messages (neurotransmitters) from inside the nerve cell to the surface where the neurotransmitters are released. The vesicles then are reprocessed inside the neuron and replenished with neurotransmitters.

The researchers found that botulinum disrupts this process by recognizing and binding to a specific protein receptor, called synaptotagmin, which is an important component of synaptic vesicles. Botulinum neurotoxin basically hijacks synaptotagmin in order to get inside the neuron, Brunger explained. Once inside, the vesicle releases the neurotoxin, which has the devastating effect of blocking the release of acetylcholine, a neurotransmitter that signals the muscle to contract.

The Brunger team also was surprised to discover that the toxicity of botulinum can be dramatically reduced by altering just one amino acid in its molecular structure. This finding suggests the possibility of designing a specific inhibitor that will prevent the neurotoxin from binding to the neuron surface.

Experimental therapies

In addition to treating botulism, the scientists said that their new findings may lead to novel remedies for several neuromuscular conditions, including uncontrolled blinking (blepharospasm), lazy eye (strabismus), involuntary neck muscle contractions (cervical dystonia) and even symptoms of cerebral palsy. Botulinum neurotoxins have become powerful therapeutic tools in the treatment of neurological, ophthalmic and other disorders caused by abnormal, excessive or inappropriate muscle contractions, Brunger said. Experimental studies are also under way that explore their use in managing chronic pain, such as headaches and migraines. Our work also may lead the way to designing modified neurotoxins as a drug d
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Contact: Mark Shwartz
mshwartz@stanford.edu
831-915-0088
Stanford University
13-Dec-2006


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