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Prion diseases such as
Creutzfeldt Jakob Disease (CJD), bovine spongiform encephalopathy (BSE),
chronic wasting disease (CWD), and scrapie are fatal, infectious,
neurodegenerative diseases that occur in humans and other mammalian
species. The conversion of a normal
host prion protein (PrP) into a protease-resistant state (PrPres) is the most
specific biochemical alteration in individuals affected by prion
disease. A rapid and sensitive
diagnostic test for early detection of prion disease is urgently needed to
help control the spread of prion diseases such as CWD and BSE throughout the
world. Such a test could be used to
identify newly infected cases, facilitating public health programs aimed at
eradicating these diseases. Tests based on measurement of
prion infectivity are highly sensitive but slow, taking months to
complete. In contrast, tests based on
PrPres detection are rapid, but less sensitive than bioassay. Biochemical amplification of PrPres could
in principle be used to increase the sensitivity of tests based on PrPres
detection, such as the standard protease digestion-Western blot assay, filter
retention assay, ELISA, or conformation dependent assay. Researchers at The major commercial
application of this discovery is enhanced sensitivity for prion disease
diagnostic testing. Other potential
applications include development of novel therapeutic and disinfectant agents
effective against infectious prions. These findings are claimed in
the issued United States Patent No. 7,407,760, and in the published United
States Patent Application Nos. 10/553,591 and 12/090,101. We are seeking an industrial partner to
further refine and market this technology. (Ref: J230) |
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«Technology Transfer Office : Sponsored Projects : Dartmouth College |
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11 Rope Ferry Road #6210 |
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Hanover, NH 03755-1404 |
Phone: (603) 646-3027 |
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Fax: (603) 646-3670 |
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