PPT-Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine

Author : rosemary | Published Date : 2023-09-06

Piccardo P Cervenakova L Vasilyeva I Yakovleva O Bacik I Cervenak J et al Candidate Cell Substrates Vaccine Production and Transmissible Spongiform Encephalopathies

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Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine: Transcript

Piccardo P Cervenakova L Vasilyeva I Yakovleva O Bacik I Cervenak J et al Candidate Cell Substrates Vaccine Production and Transmissible Spongiform Encephalopathies Emerg Infect Dis 2011171222622269 httpsdoiorg103201eid1712110607. 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.. Ovary – Cyst 1 Ovary – Cyst cysts increase with age, and the walls become so thin that identifying features are lost. The pathogenesis of ovarian cysts is often unknown; however, in mice s 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. Cosivi O, Grange J, Daborn C, Raviglione M, Fujikura T, Cousins D, et al. Zoonotic Tuberculosis due to Mycobacterium bovis in Developing Countries. Emerg Infect Dis. 1998;4(1):59-70. https://doi.org/10.3201/eid0401.980108. Jalava K, On SL, Harrington CS, Andersen LP, Hänninen M, Vandamme P. A Cultured Strain of "Helicobacter heilmannii," a Human Gastric Pathogen, Identified as H. bizzozeronii: Evidence for Zoonotic Potential of Helicobacter. Emerg Infect Dis. 2001;7(6):1036-1038. https://doi.org/10.3201/eid0706.010622. 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. Seuberlich T, Gsponer M, Drögemüller C, Polak MP, McCutcheon S, Heim D, et al. Novel Prion Protein in BSE-affected Cattle, Switzerland. Emerg Infect Dis. 2012;18(1):158-159. https://doi.org/10.3201/eid1801.111225. Song D, Kang B, Lee C, Saif LJ, Ha G, Kang D, et al. Transmission of Avian Influenza Virus (H3N2) to Dogs. Emerg Infect Dis. 2008;14(5):741-746. https://doi.org/10.3201/eid1405.071471. 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. Béringue V, Herzog L, Reine F, Le Dur A, Casalone C, Vilotte J, et al. Transmission of Atypical Bovine Prions to Mice Transgenic for Human Prion Protein. Emerg Infect Dis. 2008;14(12):1898-1901. https://doi.org/10.3201/eid1412.080941. Baron T, Bencsik A, Biacabe A, Morignat E, Bessen RA. Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model. Emerg Infect Dis. 2007;13(12):1887-1894. https://doi.org/10.3201/eid1312.070635. Gonzalez D, Estrada-Franco JG, Carrara A, Aronson JF, Vasilakis N. Equine Amplification and Virulence of Subtype IE Venezuelan Equine Encephalitis Viruses Isolated during the 1993 and 1996 Mexican Epizootics. Emerg Infect Dis. 2003;9(2):162-168. https://doi.org/10.3201/eid0902.020124. Maheshwari A, Fischer M, Gambetti P, Parker A, Ram A, Soto C, et al. Recent US Case of Variant Creutzfeldt-Jakob Disease—Global Implications. Emerg Infect Dis. 2015;21(5):750-759. https://doi.org/10.3201/eid2105.142017. 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.

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Figure Legend Figure 1 Ovary Cystin a female B6C3F1N mouse from a

Figure 2 Figure 2. Western blot analyses of brain protease-resistant prion protein

PPT-Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine

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Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine: Transcript

Figure Legend Figure 1 Ovary Cystin a female B6C3F1N mouse from a

Figure 2 Figure 2. Western blot analyses of brain protease-resistant prion protein

Figure 4 Figure 4. Control measures for bovine tuberculosis based on test-and-slaughter

Figure 1 Figure 1. Dendrogram expressing similarity in whole-cell protein patterns

Figure 4 Figure 4. Neuropathology in transgenic mice following inoculation with brain

Figure Figure. Molecular typing of the pathologic prion protein from 2 cows with

Figure 3 Figure 3. Histopathologic lesions in the trachea and lungs of control

Figure 4 Figure 4. PrPSc (disease-associated form of prion protein)–specific

Figure 2 Figure 2. Representative histoblots in 4 different anteroposterior sections

Figure 4 Figure 4. Brain lesion profiles (left panels) and disease-associated

Figure 6 Figure 6. Representative histopathologic changes of brains of infected

Figure 3 Figure 3. Results of histopathologic and immunohistochemical analyses for a US

Figure 7 Figure 7. Abnormal isoform of host-encoded prion protein (PrPSc) deposition

PPT-Figure 1 Figure 1.&nbsp;Histopathologic analysis of transgenic mouse expressing bovine

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Figure 1 Figure 1.&nbsp;Histopathologic analysis of transgenic mouse expressing bovine: Transcript

Figure Legend Figure 1 Ovary Cystin a female B6C3F1N mouse from a

Figure 2 Figure 2.&nbsp;Western blot analyses of brain protease-resistant prion protein

Figure 4 Figure 4.&nbsp;Control measures for bovine tuberculosis based on test-and-slaughter

Figure 1 Figure 1.&nbsp;Dendrogram expressing similarity in whole-cell protein patterns

Figure 4 Figure 4. Neuropathology in transgenic mice following inoculation with brain

Figure Figure.&nbsp;Molecular typing of the pathologic prion protein from 2 cows with

Figure 3 Figure 3.&nbsp;Histopathologic lesions in the trachea and lungs of control

Figure 4 Figure 4.&nbsp;PrPSc (disease-associated form of prion protein)–specific

Figure 2 Figure 2.&nbsp;Representative histoblots in 4 different anteroposterior sections

Figure 4 Figure 4.&nbsp;Brain lesion profiles (left panels) and disease-associated

Figure 6 Figure 6.&nbsp;Representative histopathologic changes of brains of infected

Figure 3 Figure 3. Results of histopathologic and immunohistochemical analyses for a US

Figure 7 Figure 7.&nbsp;Abnormal isoform of host-encoded prion protein (PrPSc) deposition

PPT-Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine

Figure 1 Figure 1. Histopathologic analysis of transgenic mouse expressing bovine: Transcript

Figure 2 Figure 2. Western blot analyses of brain protease-resistant prion protein

Figure 4 Figure 4. Control measures for bovine tuberculosis based on test-and-slaughter

Figure 1 Figure 1. Dendrogram expressing similarity in whole-cell protein patterns

Figure Figure. Molecular typing of the pathologic prion protein from 2 cows with

Figure 3 Figure 3. Histopathologic lesions in the trachea and lungs of control

Figure 4 Figure 4. PrPSc (disease-associated form of prion protein)–specific

Figure 2 Figure 2. Representative histoblots in 4 different anteroposterior sections

Figure 4 Figure 4. Brain lesion profiles (left panels) and disease-associated

Figure 6 Figure 6. Representative histopathologic changes of brains of infected

Figure 7 Figure 7. Abnormal isoform of host-encoded prion protein (PrPSc) deposition