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A prion / ˈ p r iː ɒ n / ⓘ is a misfolded protein that induces misfolding in normal variants of the same protein, leading to cellular death.Prions are responsible for prion diseases, known as transmissible spongiform encephalopathy (TSEs), which are fatal and transmissible neurodegenerative diseases affecting both humans and animals.
Antiprion drugs are drugs that work against prions. The discovery of antiprion drugs is a priority because prion diseases are untreatable and fatal. [1] Therefore, it is a therapeutic priority to find effective anti-prion drugs. [citation needed]
The subsequent demonstration that human prion diseases were transmissible reinforced the importance of spongiform change as a diagnostic feature, reflected in the use of the term "spongiform encephalopathy" for this group of disorders. Prions appear to be most infectious when in direct contact with affected tissues.
The infectious agent is a misfolded form of a host-encoded protein called prion (PrP). Prion proteins are encoded by the Prion Protein Gene . [22] The two forms of prion are designated as PrP c, which is a normally folded protein, and PrP sc, a misfolded form which gives rise to the disease.
The term prion comes from "proteinaceous infectious particle". [ 11 ] [ 12 ] Unlike other infectious agents such as viruses, bacteria, and fungi, prions do not contain nucleic acids ( DNA or RNA ). Prions are mainly twisted isoforms of the major prion protein (PrP), a naturally occurring protein with an uncertain function.
This can arise from genetic factors, infection from external source, or spontaneously for reasons unknown. Accumulation of PrP Sc corresponds with progression of neurodegeneration and is the proposed cause. Some PRNP mutations lead to a change in single amino acids (the building-blocks of proteins) in the prion protein. Others insert additional ...
The prion-rich bead fraction is subsequently harvested and tested. [10] Commonly tested tissues are brain homogenates and lymph tissues; however, prions have also been detected in skin and blood samples. [11] [12] [13] Certain tissues can be difficult to test for prions. For example, blood samples tend to have low levels of circulating ...
It opens a great promise for development of a highly sensitive detection of PrP Sc, and for understanding the molecular basis of prion replication. Indeed, PMCA has been used by various groups to PrP Sc in blood of animals experimentally infected with prions during both the symptomatic [9] and pre-symptomatic phases [10] as well as in urine. [11]