Abstract
While agent host-range and strain properties convinced early researchers of a viral etiology, the once unorthodox postulate that prion transmission occurs by conformational corruption of host-encoded cellular prion protein (PrPC) by a pathogenic isoform (PrPSc) is now widely accepted. Indeed, conformational templating is increasingly understood to be a general mechanism of protein-mediated information transfer and pathogenesis. The high infectivity of prions, their capacity to cause neurodegeneration in genetically tractable animal models, as well as the ability to culture prions in cells, or under cell-free conditions using defined components, provide finely controlled experimental settings in which to elucidate general mechanisms for all diseases involving protein conformational templating, and thus to develop integrated therapeutic approaches.
Highlights
While agent host-range and strain properties convinced early researchers of a viral etiology, the once unorthodox postulate that prion transmission occurs by conformational corruption of hostencoded cellular prion protein (PrPC) by a pathogenic isoform (PrPSc) is widely accepted
Once the leading cause of death among the Fore people in Papua New Guinea, caused by mortuary feasting; the global bovine spongiform encephalopathy (BSE) epidemic, and its subsequent zoonotic transmission in the form of variant Creutzfeldt Jakob disease, caused by prion contamination of cattle and human food, respectively; and repeated examples of large-scale animal prion disease epidemics caused by contaminated animal vaccines
Prion strain diversity is well documented for scrapie, BSE, and human prions, and most recently chronic wasting disease (CWD)
Summary
Prion Research Center (PRC) and the Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado, United States of America. While agent host-range and strain properties convinced early researchers of a viral etiology, the once unorthodox postulate that prion transmission occurs by conformational corruption of hostencoded cellular prion protein (PrPC) by a pathogenic isoform (PrPSc) is widely accepted. Conformational templating is increasingly understood to be a general mechanism of proteinmediated information transfer and pathogenesis. The high infectivity of prions, their capacity to cause neurodegeneration in genetically tractable animal models, as well as the ability to culture prions in cells, or under cell-free conditions using defined components, provide finely controlled experimental settings in which to elucidate general mechanisms for all diseases involving protein conformational templating, and to develop integrated therapeutic approaches
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