Fast and Seneitive Human Prion Disease Blood Test Prescribed by NIH

Scientists from the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health (NIH), report that they have developed a method—10,000

Scientists from the National Institute of Allergy and Infectious Diseases (NIAID), part of the National Institutes of Health (NIH), report that they have developed a method—10,000 times more sensitive than other methods—to detect variant Creutzfeldt-Jacob disease (vCJD) in blood plasma. vCJD is a type of prion disease in humans that leads to brain damage and death. The NIAID researchers also used the test to rapidly detect scrapie, a prion disease of sheep, in infected hamsters, some pre-symptomatic.

Prion diseases, also known as transmissible spongiform encephalopathies, are difficult to diagnose, untreatable and ultimately fatal. Scientists believe disease-causing prions are abnormal infectious clusters of prion protein molecules. Normally, prion protein molecules exist in every mammal in an unclustered, harmless form. In prion diseases, tissue damage leaves microscopic sponge-like holes in the brain. Along with vCJD and scrapie, other forms of prion disease include chronic wasting disease in deer, elk and moose, and bovine spongiform encephalopathy, also known as mad cow disease.

New Form of Prion Disease That Damages Brain Arteries Found
A new form of the disease in mice that does not cause the sponge-like brain deterioration typically seen in prion diseases has been observed by NIH scientists.

Because animals and people can be infected for years before symptoms of disease appear, scientists have tried to develop a rapid and sensitive screening tool to detect prion diseases in blood, which would assist in efforts to prevent the spread of prion diseases among and between species, via the blood supply or otherwise.

Collaborating with scientists from Switzerland-based Prionics AG, the NIAID group combined an antibody-based approach with an improved real-time quaking-induced protein conversion (RT-QuIC) reaction. RT-QuIC, developed in recent years, detects when normal prion protein converts to an abnormal form (http://www.niaid.nih.gov/news/newsreleases/2010/Pages/prionCaughey.aspx). The resulting test—which they call enhanced QuIC (eQuIC)—improves prospects for routinely detecting low levels of abnormal prions in tissues, fluids or environmental samples such as soil. The group plans to study eQuIC as a potential tool to diagnose various prion diseases in different animals.

Evolutionary Origins of Prion Disease Gene Unraveled
The evolutionary origin of the prion gene that is responsible for causing diseases such as mad cow disease has been uncovered

Source-Eurekalert

Prion Disease can Spread Through Faeces of Deer: Study
Brain-destroying prion disease can spread among deer through faeces shed by animals which have been infected by the deadly pathogen but are not sick, a study published on Wednesday suggests.

Research Says Gene Mutation Alone Causes Transmissible Prion Disease
Mutations associated with prion diseases are sufficient to cause a transmissible neurodegenerative disease, according to Whitehead researchers.