期刊
PATHOGENS
卷 6, 期 3, 页码 -出版社
MDPI
DOI: 10.3390/pathogens6030035
关键词
prion; cervids; PMCA; RT-QuIC; diagnosis
类别
资金
- North American Deer Farmers Association
- North American Elk Breeders Association
Since chronic wasting disease (CWD) was first identified nearly 50 years ago in a captive mule deer herd in the Rocky Mountains of the United States, it has slowly spread across North America through the natural and anthropogenic movement of cervids and their carcasses. As the endemic areas have expanded, so has the need for rapid, sensitive, and cost effective diagnostic tests-especially those which take advantage of samples collected antemortem. Over the past two decades, strategies have evolved from the recognition of microscopic spongiform pathology and associated immunohistochemical staining of the misfolded prion protein to enzyme-linked immunoassays capable of detecting the abnormal prion conformer in postmortem samples. In a history that parallels the diagnosis of more conventional infectious agents, both qualitative and real-time amplification assays have recently been developed to detect minute quantities of misfolded prions in a range of biological and environmental samples. With these more sensitive and semi-quantitative approaches has come a greater understanding of the pathogenesis and epidemiology of this disease in the native host. Because the molecular pathogenesis of prion protein misfolding is broadly analogous to the misfolding of other pathogenic proteins, including A beta and alpha-synuclein, efforts are currently underway to apply these in vitro amplification techniques towards the diagnosis of Alzheimer's disease, Parkinson's disease, and other proteinopathies. Chronic wasting disease-once a rare disease of Colorado mule deer-now represents one of the most prevalent prion diseases, and should serve as a model for the continued development and implementation of novel diagnostic strategies for protein misfolding disorders in the natural host.
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