PPT-Figure 1 Figure 1. . Detection of disease-related prion protein (PrPSc) in brains of

Wadsworth J Joiner S Linehan JM BalkemaBuschmann A Spiropoulos J Simmons MM et al Atypical Scrapie Prions from Sheep and Lack of Disease in Transgenic Mice Overexpressing Human Prion Protein Emerg Infect Dis 2013191117311739 httpsdoiorg103201eid1911121341. Prion. Sarah . Themel. This is your brain…. This is Your . B. rain on . P. rions. What is a Prion?. Prion diseases are called spongiform encephalopathies. They impair brain functions, leading to both mental and physical deterioration over short periods of time.. Christina Hill . Department of Biological Sciences, York College of Pennsylvania. Project Summary. Bovine Spongiform Encephalopathy (BSE) and Natural Scrapie are prion diseases that result from the mis-folding of proteins in the brain. One mis-folded protein can cause other proteins to mis-fold creating florid plaques that can affect motor function and decrease lifespan. Prion diseases can be transferred to animal species that are not naturally susceptible to these diseases through gene transfer. Research shows that brain plaque isolates from animals infected with prion diseases can be collected and inserted into the brains of transgenic mice. In the proposed experiment, 10 (OvTgPrP4) transgenic mice will be injected with normal saline, 10 with BSE isolates and 10 with Natural Scrapie isolates. Inoculated transgenic mice are observed for changes in motor function each week for course of their lifespan. After expiration, the mice can be dissected and their brain removed. The removed brains would be paraffin-embedded for microtome sectioning. These sections will be stained using Immunohistochemistry to look for the presence of florid plaques associated with the respective disease. Isolates from each mouse brain will also be tested for infection using a Sandwich ELISA test. Infection in all mice inoculated with the respective diseases should be found, as well as a decrease in motor dysfunction and lifespan. Effective transmission of prion diseases to species without natural susceptibility can allow for more effective medical models to be developed and increased knowledge of these diseases.. Creutzfeldt. -Jakob Disease. Human equivalent of mad cow . disease. Rare. , degenerative, fatal disease. Approximately 1 case per million per year. Typically people are diagnosed around age 60 . CJD belongs to a family of human and animal diseases known as the transmissible spongiform . Argument Mini-Unit. PowerPoint adapted by Amy . Vujaklija. and Jean . Wolph. from materials developed by Beth . Rimer. , Ohio Writing Project, for the National Writing Project i3 College Ready Writers Program, funded by the Department of Education.. Anne Busch. Transmission of Prion diseases. Infectious prion disease spread through: . Ingestion of diseased tissue or body fluid . Inhalation of aerosols (in mice) . Transmission: donor prion enters the recipient cell → host prion binds to the ends of amyloid prion (template) → host prion adopts amyloid form . Dr. Mourad Tayebi . D.V.M (. Hons. ) . M.Sc. Ph.D . Senior Lecturer; University of Surrey / Founder and CSO; PrioCam LLC (USA). International Congress on Neuroimmunology and Therapeutics. July 20-22, 2015 San Francisco, California, USA. Page 1 of 5Cand PrPSc in infection Effects in Blocking Neural Synapses and its Comprehensive ObservationAhnaf Ilman1 and Md Abu Syed21Department of Science Dhaka Residential Model College Bangladesh2D (Credit Hours-3+1). Prions. diseases. Transmissible spongiform encephalopathies (TSEs). Infectious . amyloidosis. Unconventional slow virus degenerative . encephalopathies. Introduction. Prions. diseases/ TSE are a family of: . Carlos Francisco Mendoza. Human Prion Diseases. Comparison of Prp. C. and . Prp. Sc. Evidence Supports the Prion Hypothesis. Genetic . Polymorphism. RPSA Polymorphisms have no direct influence on susceptibility to sporadic CJD. Torres J, Andréoletti O, Lacroux C, Prieto I, Lorenzo P, Larska M, et al. Classical Bovine Spongiform Encephalopathy by Transmission of H-Type Prion in Homologous Prion Protein Context. Emerg Infect Dis. 2011;17(9):1636-1644. https://doi.org/10.3201/eid1709.101403. Babelhadj B, Di Bari M, Pirisinu L, Chiappini B, Gaouar S, Riccardi G, et al. Prion Disease in Dromedary Camels, Algeria. Emerg Infect Dis. 2018;24(6):1029-1036. https://doi.org/10.3201/eid2406.172007. Diack AB, Ritchie D, Peden AH, Brown D, Boyle A, Morabito L, et al. Variably Protease-Sensitive Prionopathy, a Unique Prion Variant with Inefficient Transmission Properties. Emerg Infect Dis. 2014;20(12):1969-1979. https://doi.org/10.3201/eid2012.140214. Angers RC, Seward TS, Napier D, Green M, Hoover E, Spraker T, et al. Chronic Wasting Disease Prions in Elk Antler Velvet. Emerg Infect Dis. 2009;15(5):696-703. https://doi.org/10.3201/eid1505.081458. 2. CNS Infection - Meninges. CNS infections: most are due to sepsis. Pathogenesis:. Hematogenous spread (most common) . Traumatic implantation . Local extension from nearby infection . Ascent of peripheral nerve.