Prions and Encephalopathies: Difference between revisions

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==References==
==References==
[Sample reference] [http://ijs.sgmjournals.org/cgi/reprint/50/2/489 Takai, K., Sugai, A., Itoh, T., and Horikoshi, K. "''Palaeococcus ferrophilus'' gen. nov., sp. nov., a barophilic, hyperthermophilic archaeon from a deep-sea hydrothermal vent chimney". ''International Journal of Systematic and Evolutionary Microbiology''. 2000. Volume 50. p. 489-500.]
[1] [Baxter, H., Campbell, G., Whittaker, A., Jones, C., Aitken, A., Simpson, A., Casey, M., Bountiff, L., Gibbard, L., and Baxter, R., 2005, Elimination of transmissible spongiform encephalopathy infectivity and decontamination of surgical instruments by using radio-frequency gas-plasma treatment, Journal General Virology, vol 86, pg 2393-2399]
[http://link.springer.com/content/pdf/10.1385%2F1-59259-766-1%3A517 Priola, S., and Vorberg, I. "Molecular Aspects of Disease Pathogenesis in the Transmissible Spongiform Encephalopathies". ''Methods in Molecular Biology''. 2004. Volume 268. p. 517-540.]
 


Edited by student of [mailto:slonczewski@kenyon.edu Joan Slonczewski] for [http://biology.kenyon.edu/courses/biol238/biol238syl09.html BIOL 238 Microbiology], 2009, [http://www.kenyon.edu/index.xml Kenyon College].
Edited by student of [mailto:slonczewski@kenyon.edu Joan Slonczewski] for [http://biology.kenyon.edu/courses/biol238/biol238syl09.html BIOL 238 Microbiology], 2009, [http://www.kenyon.edu/index.xml Kenyon College].


<!--Do not edit or remove this line-->[[Category:Pages edited by students of Joan Slonczewski at Kenyon College]]
<!--Do not edit or remove this line-->[[Category:Pages edited by students of Joan Slonczewski at Kenyon College]]

Revision as of 18:32, 23 April 2013

Introduction

Digital representation of an incorrectly folded prion protein. Image created by the Mayo Clinic.

“Prion” is the name given to a class of proteins which can cause severe neurological diseases in a host of mammalian species, including humans. These disorders are a result of misfolding of naturally found proteins in host tissue. While the exact mechanisms of transmission from protein to protein are not completely understood, the general mechanism of infection is that existing misfolded proteins cause the same misfolding in these existing normal proteins. These misfolded proteins are extremely resilient– they are resistant to extreme temperatures, both dry and wet, as well as radiation (Yam, 2011). The accumulation of diseased prions in mammalian tissues, commonly in the nervous system, causes Transmissible Spongiform Encephalopathies (TSEs). This name reflects the appearance of the infected animal’s tissues after infection – the brain and related tissue resemble sponges because of the disintegration of the tissue by the misfolded protein. In general, these disorders are characterized by a long incubation period, followed by an aggressive and always fatal loss of brain and nervous system function. In addition, these diseases do not induce an inflammatory response in the diseased individual (CDC, 2013).2




Transmissible Spongiform Encephalopathies in Animals


Include some current research in each topic, with at least one figure showing data.

A domestic sheep in the later stages of Scrapie. Image from http://academics.wellesley.edu/Chemistry/Chem101/aspirin/1mouton%20scrapie.jpg

The Prion Protein and Mechanism of Infection


Include some current research in each topic, with at least one figure showing data.

Interspecific Barriers and Predictors of Susceptibility


Include some current research in each topic, with at least one figure showing data.

Model of a healthy host prion protein proposed by Hagiwara et al. (2012)
Different models of pathogenic prion proteins proposed by Hagiwara et al. (2012)

Treatment


Overall paper length should be 3,000 words, with at least 3 figures.

References

[1] [Baxter, H., Campbell, G., Whittaker, A., Jones, C., Aitken, A., Simpson, A., Casey, M., Bountiff, L., Gibbard, L., and Baxter, R., 2005, Elimination of transmissible spongiform encephalopathy infectivity and decontamination of surgical instruments by using radio-frequency gas-plasma treatment, Journal General Virology, vol 86, pg 2393-2399]


Edited by student of Joan Slonczewski for BIOL 238 Microbiology, 2009, Kenyon College.