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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.
PMCA was originally developed to, in vitro, mimic prion replication with a similar efficiency to the in vivo process, but with accelerated kinetics. [1] PMCA is conceptually analogous to the polymerase chain reaction - in both systems a template grows at the expense of a substrate in a cyclic reaction, combining growing and multiplication of the template units.
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 abnormal protein PrP Sc accumulates in the brain and destroys nerve cells, which leads to the mental and behavioral features of prion diseases. [citation needed] Several other changes in the PRNP gene (called polymorphisms) do not cause prion diseases but may affect a person's risk of developing these diseases or alter the course of the ...
The agent is thought to be much smaller than the smallest known virus. Prions multiply by causing normally folded proteins of the same type to take on their abnormal shape, which then go on to do the same, in a kind of chain reaction. These abnormal proteins are gradually accumulated in the body, especially in nerve cells, which subsequently die.
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