SYNTHETIC PRION CAUSES NEUROLOGICAL DISEASE IN MICE

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Scientists have produced a prion protein that can trigger

the development of a neurological disorder in mice that is

similar to "mad cow" disease, according to a new study

supported by the National Institute on Aging (NIA), a part

of the National Institutes of Health. The findings

demonstrate that prions, an unusual class of infectious

proteins, can make copies of themselves without the

presence of viral DNA or RNA, damage brain tissue, and

cause neurological diseases.

The work by Nobel Laureate Stanley B. Prusiner, M.D., and

colleagues at the University of California, San Francisco,

and Heinrich-Heine Universitat in Germany, appears in the

July 30, 2004, issue of "Science". For the study, Dr.

Prusiner and his colleagues produced prion protein

fragments in bacteria, folded them into larger protein

structures called amyloid fibrils, and then injected them

into the brains of susceptible mice. The mice began

exhibiting symptoms of disease in their central nervous

systems between 380 and 660 days after they were given the

synthetic prion proteins. The amyloid form of the prion

protein, which is thought to cause prion disease, was also

found in the brains of the diseased mice. The researchers

then administered brain extracts from these animals to

another group of mice, which subsequently developed similar

symptoms 90 to 150 days later. The disorder seems to be

distinct from that caused by other known strains of prions,

suggesting that the synthetic prion didn't merely activate

a pre-existing prion in these mice and that the synthesized

prion protein itself is sufficient to make infectious and

disease-causing prions.

Prusiner received the 1997 Nobel Prize in physiology or

medicine for his discovery of prions. Unlike viruses,

bacteria, fungi and parasites, prions contain no DNA or

RNA. Instead, they are a type of protein normally found

within cells in humans and other organisms. In some cases,

the structure of prions can change into a disease-causing

form. These abnormal proteins appear to convert other,

normal prions to the abnormal shape. Many scientists now

believe this conversion process leads to several dementing

diseases in humans, including Creutzfeldt-Jakob disease.

Similar diseases in animals include bovine spongiform

encephalopathy ("mad cow" disease) in cattle and scrapie in

sheep. Abnormal, misfolded proteins contribute to other

age-related neurological diseases such as Alzheimer's and

Parkinson's diseases, and so these new findings may provide

insights into the cause and possible prevention of other

brain disorders.

EDS: Andrew Monjan, Ph.D., of the NIA's Neuroscience and

Neuropsychology of Aging Program is available to discuss

this finding. For an interview, please phone (301) 496-

1752.

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