Research Progress of Prion Characteristics and Pathogenesis

Abstract

Prions are infectious proteins that cause disease in variable species of animals, including human being. The normal, cellular protein PrP (PrPC) is converted into PrPSc through a post translational process during which it acquires a high β-sheet content which made the protein resistant to degradation by proteinase K due to its PrP 27-30 domain that increase its half-life to >48 hours as compared to that of the normal 3-6 hours, its stay leads to self-propagation and toxicity. The disease pathology is associated with many disturbances mainly in central nervous system which resulted from increased oxidative stress and mitochondrial dysfunction, disturbance of iron metabolism, alteration of calcium metabolism, increases of inflammatory cytokines, chemokine’s and nuclear factor-kappa β activity. The entire process creates a spongy hole inside the nervous system which leads to condition called encephalopathy. The agent cause scrapie in sheep and goats, bovine spongiform encephalopathy (BSE) in cattle (known as mad cow disease), transmissible mink encephalopathy (TME) in mink, chronic wasting disease (CWD) in white tailed deer, elk, mule deer and moose, feline spongiform encephalopathy in cats, exotic ungulate encephalopathy (EUE) in Nyala and Oryx. In humans it causes Creutzfeldt-Jakob disease (CJD) and its varieties, Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (sFI) and Kuru. Prion diseases have zoonotic and interspecies transmission. Banning Meat bone meal and culling infected animals are recommended.