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Review
Human Prion Diseases
Author(s): Tvisha Joshi*
The functions of these normal prion proteins are still not completely understood. The discovery of proteinaceous infectious agents by Prusiner in 1982 was sensational. All previously known pathogens contained nucleic acids, the code of life, that enabled them to reproduce. In contrast, the proteinaceous agents of disease, called prion proteins (PrP), lacked nucleic acids and propagated by binding to the functional, endogenous form of cellular prion protein (referred to as PrPC) and altering its conformation to produce the infectious disease-causing misfolded protein (referred to as PrPSc). The accumulation and aggregation of these infectious prion proteins within the brain causes destruction of neural tissue and leads to fatal spongiform encephalopathies. In this review, we present the molecular pathology of prion-based diseases. These insights are of particular importance since the p.. View More»
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