Promising new prion research.

Promising new prion research. The June 3rd issue of Science reported that research conducted by the National Institutes of Health suggests that brain damage caused by transmissible spongiform encephalopathy (TSE) infections would be lessened if the resulting abnormal prions could be prevented

from interacting with brain cells. Prions are naturally occurring proteins found in the brains of healthy humans and animals. When a human or animal contracts a TSE--such as mad cow disease in bovines, Creutzfeldt-Jakob disease in humans, and scrapie in sheep--prions begin to twist into abnormal shapes and form clumps that kill brain cells, producing symptoms including dementia and leading to certain death.

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NIH researchers, led by virologist Dr. Bruce Chesebro, bred genetically altered mice that did not have the fatty bond that allows prions to attach to brain cells. The team subsequently infected 128 of the altered mice and 70 unaltered mice with a form of scrapie, modified to infect rodents.

Although the unaltered mice sickened and died within the expected time period, the altered mice did not develop the typical symptoms and have survived for almost two years, far longer than the unaltered mice. When the researchers examined the brains of the altered mice, they discovered that the prions had mutated in a different manner than that normally associated with the disease and had not attached themselves to brain cells. In fact, the malformed prion patterns appeared similar to those found in Alzheimer's patients.

Whereas scientists studying the treatment of prion diseases currently concentrate on preventing the accumulation of malformed prions, the NIH's findings suggest that treatment research might be better directed at preventing prion clusters from binding to brain cells.