Prion diseases, also known as transmissible spongiform encephalopathies (TSE), are a class of infectious, progressive and fatal neurodegenerative disorders associated with the loss of cognitive skills and neuronal dysfunction in animals and humans.1,2 Accumulation of misfolded proteinaceous particles (prions) is regarded a hallmark feature that is necessary for progression to TSEs.3 However, it is still not entirely understood how these aggregates are formed and when or why the conversion of cellular, non-pathogenic prion protein (PrPC) into pathogenic scrapie PrP (PrPSc) occurs. Here, PRNP is linked to human prion disease.