A breakdown of the prion proteins responsible for the brain diseases as Variant Creutzfeldt-Jakob Disease (vCJD) and formerly Kuru in humans, Scrapie in sheep, Bovine Spongiform Encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids like deer and moose.
Prions (PrP) are abnormal, misfolded protein pathogens known to cause neurodegenerative
diseases such as Variant Creutzfeldt-Jakob Disease (vCJD) and formerly Kuru in humans,
Scrapie in sheep, Bovine Spongiform Encephalopathy (BSE) in cattle, and chronic wasting
disease (CWD) in cervids like deer and moose. Prion diseases are incredibly contagious and
completely fatal. Means of infection include exposure to PrP contaminated food, medical
equipment, and exposure to body fluids of infected animals such as blood and urine. Prion
diseases are protein misfolding diseases that interfere with normal function, resulting in cell
death and infection. Because prions are not viruses, bacteria or other organismal
pathogens, typical means of repelling infections are generally ineffective. Prions cannot be
killed, as they are misfolded proteins rather than full cells.
Figure 1. Prion protein in its normal form compared to the disease-causing variant.
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