Absence of toxicity in killer proteins
Toxicity in a prion-infected brain has long been assumed to be present because of infectious prion proteins. New methods were used to test this assumption.
Throughout its history, humanity has dealt with countless wars, pandemics, natural disasters, and other such cataclysms. In recent decades, a new challenge arose—prions. Prion proteins inhibit brain activity and aid neuron connections with their healthy form: PrPC (Prion Protein Cellular). However, a misfolding of such protein (PrPSc - Prion Protein Scrapie) leads to irreversible neurodegeneration, or continuous damage to the brain, inevitably leading to death. This infectious disease involves many types, two famous ones being Creutzfeldt-Jakob disease (CJD) and scrapie, all presenting the characteristics of brain damage and loss of neuronal cells. The mechanisms of each type are still heavily studied today; however, the cure is not yet found. It has long been assumed that the infectivity of prions is associated with neurotoxicity and is the cause of their fatality. Benilova and colleagues (2020) researched this theory using mice and new methods that allow the separation of infectivity and neurotoxicity.