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United States Department of Agriculture

Agricultural Research Service

Research Project: DETECTION OF TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHY AGENTS IN LIVESTOCK, WILDLIFE, AGRICULTURAL PRODUCTS, AND THE ENVIRONMENT Title: Prion Diseases

Author
item Silva, Christopher

Submitted to: Book Chapter
Publication Type: Book / Chapter
Publication Acceptance Date: August 1, 2008
Publication Date: May 1, 2009
Citation: Silva, C.J. 2009.Prion Diseases:Sequelae and Long Term Consequences of Infectious Diseases. District of Columbia:ASM Press. 442p.

Interpretive Summary: Prion diseases are a set of rare fatal brain diseases found in animals and people. A prion is a protein that changes a normal protein into a prion. This change of normal protein into prion causes disease. A prion and the normal protein are nearly the same and differ only in 3-dimensional arrangement of their atoms. There are different strains of prions. Prions are difficult to destroy. The amino acid sequence, glycosylation and GPI anchor have roles in the pathogenesis of prions and prion strains. The existence of prions challenges the assumption that a single gene makes a single protein with a single function. In microbes, prions allow the bug to grow on nitrogen poor media, so a prion does not always cause a disease. Other diseases such as Alzheimer’s and type II diabetes are similar to prion diseases. The study of prion diseases will provide insights into treating these more common prion-like diseases. Prion diseases are the only sicknesses that can be inherited from parents or result from an infection. Although prion disease cannot be cured, there is hope that prion diseases may be cured in the future.

Technical Abstract: Prion diseases comprise a set of rare fatal neurological diseases found in humans and other mammals. A prion is a protein capable of converting a normal cellular protein (PrPC) into a prion and thereby propagating an infection. A prion and PrPC differ solely in their conformation. There are different strains of prions each has a distinct and stable conformations. Prions are difficult to inactivate. The amino acid sequence, glycosylation and GPI anchor have roles in the pathogenesis of prions and prion strains. The existence of prions challenges the assumption that a single gene generates a single protein with a single function. Yeast prions facilitate the growth of the host on nitrogen poor media, so a prion is not always a pathogen. Although prions are the best known example of a protein misfolding disease, other diseases such as Alzheimer’s and type II diabetes are also associated with protein misfolding. The study of prion diseases will provide insights into these more common protein misfolding diseases. Prion diseases are the only diseases known to be both heritable and transmissible. Unfortunately, there is no effective treatment for prion diseases. There is promise that an effective treatment may be developed in the future.

Last Modified: 4/17/2014