✍️ Author: Dr Eleni Christoforidou
🕒 Approximate reading time: 4 minutes
Prions, or proteinaceous infectious particles, are unique proteins that can transmit their misfolded shape onto normal variants of the same protein. They are the causative agents of a distinct class of neurodegenerative diseases known as prion diseases. In this blog post, we delve into what prions are, how they cause disease, and what makes them a unique class of neurodegenerative diseases.
Prions are abnormal, misfolded proteins that can induce normal proteins in the brain to also misfold. Unlike other infectious agents, prions do not contain nucleic acids, making them unique in the world of pathogens.
The primary mechanism of prion diseases involves the conversion of the normal cellular prion protein (PrPC) into the disease-associated isoform (PrPSc). This transformation is thought to occur when PrPSc comes into contact with PrPC, inducing a conformational change.
Once misfolded, the proteins aggregate into clumps that the cell cannot easily break down. These aggregates damage nerve cells and cause the many neurological symptoms associated with prion diseases, such as rapidly progressive dementia, motor dysfunction, and eventually death.
Several features set prion diseases apart from other neurodegenerative disorders. First, prion diseases are transmissible, meaning they can spread from organism to organism, unlike other neurodegenerative diseases such as Alzheimer's or Parkinson's.
Second, prion diseases exhibit an extraordinarily long incubation period. In some cases, prion diseases may take decades to manifest clinically.
Finally, prion diseases, unfortunately, have no cure. Treatment is typically focused on alleviating symptoms and improving quality of life.
In conclusion, prion diseases represent a unique class of neurodegenerative disorders. Further research into the biology of prions could not only lead to breakthroughs in treating prion diseases but also enhance our understanding of other neurodegenerative conditions that involve protein misfolding and aggregation.