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Currently available diagnostic tests lack the sensitivity, speed or quantitative capabilities required for many important applications in medicine, agriculture, wildlife biology and research. Because prion infections can be present for decades before disease symptoms appear, a better test might create the possibility for early treatment to stop the spread of disease and prevent death. This approach is described in a paper now online in the open-access journal PLoS Pathogens. Byron Caughey, Ph.

Unraveling prion structures and biological functions

Scientists believe disease-causing prions are abnormal infectious clusters of prion protein molecules. Normally, prion protein molecules are unclustered, harmless and found in every mammal. In a process not fully understood, abnormal infectious clusters develop and can convert normal prion protein molecules into the infectious prion form; these clusters tend to gather in the brain.

Ongoing replication allows the disease to spread and damage the brain.

Infectious prions also are found outside the brain, in saliva, blood, breast milk, urine and the nasal and cerebral spinal fluids used in the study. But the concentrations of infectious prions in these bodily fluids are so low that scientists, clinicians and wildlife biologists have not been able to measure them for routine purposes.

The new assay can detect when miniscule amounts of infectious prions initiate the conversion of large amounts of normal prion protein into an abnormal form in test-tube reactions.

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By comparing the extent to which different samples can be diluted and still initiate conversion, scientists can estimate the relative infectious concentrations in the original samples. In scrapie-infected hamsters, they found surprisingly high levels of prions in nasal fluids, pointing to such fluids as possible sources of contagion in various prion diseases. Along with optimizing their existing applications in the laboratory, Dr.

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Caughey and his colleagues are teaming up with a number of other laboratories around the world to extend the practical and scientific applications of RT-QuIC. Related testing approaches might also aid the diagnoses of similar neurodegenerative protein diseases, such as Alzheimer's, Huntington's and Parkinson's diseases. Note: Content may be edited for style and length. Science News.

PRION 12222 emerging concepts

Journal Reference : Jason M. Wilham, Christina D. Ongoing replication allows the disease to spread and damage the brain.

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Infectious prions also are found outside the brain, in saliva, blood, breast milk, urine and the nasal and cerebral spinal fluids used in the study. But the concentrations of infectious prions in these bodily fluids are so low that scientists, clinicians and wildlife biologists have not been able to measure them for routine purposes. The new assay can detect when miniscule amounts of infectious prions initiate the conversion of large amounts of normal prion protein into an abnormal form in test-tube reactions.


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By comparing the extent to which different samples can be diluted and still initiate conversion, scientists can estimate the relative infectious concentrations in the original samples. In scrapie-infected hamsters, they found surprisingly high levels of prions in nasal fluids, pointing to such fluids as possible sources of contagion in various prion diseases.

Along with optimizing their existing applications in the laboratory, Dr. Caughey and his colleagues are teaming up with a number of other laboratories around the world to extend the practical and scientific applications of RT-QuIC. Related testing approaches might also aid the diagnoses of similar neurodegenerative protein diseases, such as Alzheimer's, Huntington's and Parkinson's diseases. Note: Content may be edited for style and length.

Science News.


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Journal Reference : Jason M. Wilham, Christina D. Meade-White, Lara M.


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Taubner, Andrew Timmes, Byron Caughey. ScienceDaily, 5 December Early detection is possible for prion diseases, study suggests. Retrieved November 25, from www. The infectious, misfolded protein The aggregates are associated with human diseases.