Transmissible spongiform encephalopathies

Sejvar, James J.; Schonberger, Lawrence B.; Belay, Ermias D.

doi:10.2460/javma.233.11.1705

Cited by 9 publications

(3 citation statements)

References 70 publications

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“…Transmissible spongiform encephalopathies (TSEs) are a class of fatal mammalian neurodegenerative diseases, which include Creutzfeldt-Jakob disease in humans, mad cow disease in cattle, and scrapie in sheep (Sejvar et al, 2008). TSEs result from conformational conversion of cellular prion protein (PrP C ), a glycoprotein expressed within the central nervous system, into its infectious, amyloid-like isoform (PrP Sc ) (Prusiner, 1998; Caughey and Chesebro, 2001; Collinge, 2001; Aguzzi and Polymenidou, 2004).…”

Section: Biological Contextmentioning

confidence: 99%

13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

et al. 2016

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The Y145Stop prion protein (PrP23–144), which has been linked to the development of a heritable prionopathy in humans, is a valuable in vitro model for elucidating the structural and molecular basis of amyloid seeding specificities. Here we report the sequential backbone and side-chain 13C and 15N assignments of mouse and Syrian hamster PrP23-144 amyloid fibrils determined by using 2D and 3D magic-angle spinning solid-state NMR. The assigned chemical shifts were used to predict the secondary structures for the core regions of the mouse and Syrian hamster PrP23-144 amyloids, and the results compared to those for human PrP23-144 amyloid, which has previously been analyzed by solid-state NMR techniques.

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Section: Biological Contextmentioning

confidence: 99%

13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

et al. 2016

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“…TSE or prion diseases are transmissible neurodegenerative diseases occurring in a variety of mammalian species including domestic and wild animals as well as humans [1]. Examples include scrapie in sheep, chronic wasting disease (CWD) in cervids and bovine spongiform encephalopathy (BSE) in cattle.…”

Section: Introductionmentioning

confidence: 99%

Strain Specific Resistance to Murine Scrapie Associated with a Naturally Occurring Human Prion Protein Polymorphism at Residue 171

et al. 2011

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Transmissible spongiform encephalopathies (TSE) or prion diseases are neurodegenerative disorders associated with conversion of normal host prion protein (PrP) to a misfolded, protease-resistant form (PrPres). Genetic variations of prion protein in humans and animals can alter susceptibility to both familial and infectious prion diseases. The N171S PrP polymorphism is found mainly in humans of African descent, but its low incidence has precluded study of its possible influence on prion disease. Similar to previous experiments of others, for laboratory studies we created a transgenic model expressing the mouse PrP homolog, PrP-170S, of human PrP-171S. Since PrP polymorphisms can vary in their effects on different TSE diseases, we tested these mice with four different strains of mouse-adapted scrapie. Whereas 22L and ME7 scrapie strains induced typical clinical disease, neuropathology and accumulation of PrPres in all transgenic mice at 99-128 average days post-inoculation, strains RML and 79A produced clinical disease and PrPres formation in only a small subset of mice at very late times. When mice expressing both PrP-170S and PrP-170N were inoculated with RML scrapie, dominant-negative inhibition of disease did not occur, possibly because interaction of strain RML with PrP-170S was minimal. Surprisingly, in vitro PrP conversion using protein misfolding cyclic amplification (PMCA), did not reproduce the in vivo findings, suggesting that the resistance noted in live mice might be due to factors or conditions not present in vitro. These findings suggest that in vivo conversion of PrP-170S by RML and 79A scrapie strains was slow and inefficient. PrP-170S mice may be an example of the conformational selection model where the structure of some prion strains does not favor interactions with PrP molecules expressing certain polymorphisms.

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“…The prototypical animal prionopathy is scrapie, a TSE affecting sheep and goats, from which the term PrPscrapie (PrPsc) is derived. Other animal TSEs include transmissible mink encephalopathy, chronic wasting disease in North American elk and deer, and bovine spongiform encephalopathy (BSE) in cattle ( Sejvar et al, 2008b ). Human prionopathies include kuru, fatal familial insomnia, Gerstman–Straussler–Scheinker syndrome, and CJD ( Brown and Mastrianni, 2010 ).…”

Section: Epidemiology Of Viral Infections Of the Nervous Systemmentioning

confidence: 99%

Neuroepidemiology and the epidemiology of viral infections of the nervous system

Sejvar

2014

Neurovirology

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Viral infections result in a tremendous burden of neurologic illness worldwide. Although many viral etiologies of neurologic infectious disease have been recently controlled through vaccination and other public health measures, the emergence of new pathogens and the re-emergence of previously controlled pathogens remain significant global public health challenges. One of the fundamental bases for understanding the dynamics of viral nervous system infections is through epidemiology – the science of assessing patterns of disease in populations and the factors that influence these patterns. Neuroepidemiology is a discipline that applies epidemiologic principles and practices to neurologic disease. There are several characteristics of neurologic illness that necessitate the subdiscipline of neuroepidemiology. This chapter reviews some of the basic terms and concepts of neuroepidemiology, including epidemiologic analysis and studies. It then applies these concepts to infections of the nervous system, including encephalitis, aseptic meningitis, acute myelitis, prion diseases, and slow virus infections. The chapter then addresses the epidemiology of emerging and re-emerging viral neurologic diseases as well as the factors driving these emergences. The epidemiology of viral nervous system diseases will undoubtedly continue to change and expand, and as we gain a better understanding of this epidemiology and the pathophysiology of viral infections, this will hopefully lead to improved surveillance, diagnostic, treatment, and prevention strategies for these illnesses.

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Transmissible spongiform encephalopathies

Cited by 9 publications

References 70 publications

13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

Strain Specific Resistance to Murine Scrapie Associated with a Naturally Occurring Human Prion Protein Polymorphism at Residue 171

Neuroepidemiology and the epidemiology of viral infections of the nervous system

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