Abstract
Prion diseases are transmissible neurodegenerative conditions affecting human and a wide range of animal species. The pathogenesis of prion diseases is associated with the accumulation of aggregates of misfolded conformers of host-encoded cellular prion protein (PrPC). Animal prion diseases include scrapie of sheep and goats, bovine spongiform encephalopathy (BSE) or mad cow disease, transmissible mink encephalopathy, feline spongiform encephalopathy, exotic ungulate spongiform encephalopathy, chronic wasting disease of cervids and spongiform encephalopathy of primates. Although some cases of sporadic atypical scrapie and BSE have also been reported, animal prion diseases have basically occurred via the acquisition of infection from contaminated feed or via the exposure to contaminated environment. Scrapie and chronic wasting disease are naturally sustaining epidemics. The transmission of BSE to human has caused more than 200 cases of variant Cruetzfeldt-Jacob disease and has raised serious public health concerns. The present review discusses the epidemiology, clinical neuropathology, transmissibility and genetics of animal prion diseases.
Highlights
Prion diseases are transmissible protein misfolding disorders in which misfolding of a host-encoded prion protein (PrP) occurs
Chronic Wasting Disease (CWD) has been detected in USA in areas far from the original endemic area and raised several questions: Whether the infectivity has been transported to these areas illegally in the form of tainted materials or infected animals or by some another way, whether the scrapie agent has adapted to cause CWD by repeated natural passages into the deer, or if the PrPC conversion in cervids is proficient enough to result in the sporadic emergence of the disease, which may in turn establish the epidemic by horizontal transmission
Animal prion diseases other than scrapie and CWD have been controlled by the withdrawal of source of contamination from animals’ diet
Summary
Prion diseases are transmissible protein misfolding disorders in which misfolding of a host-encoded prion protein (PrP) occurs. CWD has been detected in USA in areas far from the original endemic area and raised several questions: Whether the infectivity has been transported to these areas illegally in the form of tainted materials or infected animals or by some another way, whether the scrapie agent has adapted to cause CWD by repeated natural passages into the deer, or if the PrPC conversion in cervids is proficient enough to result in the sporadic emergence of the disease, which may in turn establish the epidemic by horizontal transmission. As most of the FSE cases occurred in parallel to the BSE epidemic, exposure of affected cats to feed contaminated with PrPBSE was taken as causative of the disease. Mice inoculated with brain homogenates from cats with FSE and cattle with BSE developed a TSE with similar profiles of neuropathological lesions and incubation periods. In these naturally and experimentally infected lemurs, immunohistochemical examination showed similar staining patterns and the distribution of PrPres in the brain, spinal cord, tonsils, spleen and various sections of the gut and gut-associated lymphatic tissues [17,66]
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