Location: Virus and Prion Research
Title: The diagnosis of the prion diseases of animalsAuthor
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Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 2/18/2019 Publication Date: 5/8/2019 Citation: Greenlee, J.J. 2019. The diagnosis of the prion diseases of animals [abstract].2019 Tri-State plus One Histology Symposium. 05/08/2019. Interpretive Summary: Technical Abstract: The transmissible spongiform encephalopathies (TSE’s) or prion diseases are fatal neurodegenerative diseases caused by accumulation of a misfolded form of the prion protein called PrPSc. Historically, these diseases were diagnosed microscopically by examining HE stained brain sections for the presence of neuron degeneration, gliosis, and spongiform change, which can appear as either small round empty spaces in the neuropil or vacuoles present within neuron cell bodies. Identification of the TSE’s as diseases of the prion protein opened new avenues for antibody based diagnostic tests such as western blot and immunohistochemistry. Immunohistochemistry is considered the gold standard in the diagnosis of prion diseases; however, much effort has been put into new diagnostic or screening methods that can be performed on live animals. In our lab we have developed two screening technologies for prion diseases that utilize examination of the retinas of live animals: Optical coherence tomography that measures retinal thickness and electroretinograms that measures the electrical impulses generated in the eye as visual stimulus is converted into a nerve signal. Both of these techniques identify animals incubating prion diseases prior the onset of clinical signs. Microscopic evaluation of retinal tissues and the use of tissue specific cell markers was instrumental in the process of validating these techniques for the identification of prion diseases in live animals. |
