Chapter 22 : Prions and Prion Diseases

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Prions are generally regarded as the most reliable markers of so-called prion diseases. With the advent of the protein-only concept of the transmission of prion diseases, which is predicated on the idea that prions are the infectious agents causing prion disease, and with the 1997 Nobel Prize for Medicine awarded for the prion protein concept, prions have firmly asserted their inclusion in the club of infectious agents, along with bacteria, viruses, fungi, and parasites, the club's traditional members. The essence of the protein-only theory is that the abnormal prion enters the organism and converts the host’s normal prions into abnormal prions. The efficiency of the conversion is influenced by the degree of amino acid sequence homology between the two PrPs involved, so that the greater the degree of homology, the greater the rate of conversion. Several studies suggest that white blood cells may be involved in the process. It was observed that gut-associated macrophages initially remove transmissible spongiform encephalopathy (TSE) infectivity, but once their ability to remove the infectivity completely is overcome, macrophages may facilitate the spread of infectivity. Regulatory measures introduced to prevent the spread of TSEs to humans and other animal species are likely to stay. It is possible, however, that more research and better tests will more adequately characterize risk, which in turn may lead to a gradual loosening of some of the currently existing restrictions following a carefully performed risk assessment.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22

Key Concept Ranking

Enzyme-Linked Immunosorbent Assay
Bovine Spongiform Encephalopathy
Chronic Wasting Disease
Transmissible Spongiform Encephalopathies
Peyer's Patches
White Blood Cells
Prion Proteins
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Image of Figure 1.
Figure 1.

Common approaches to detecting TSEs.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
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Image of Figure 2.
Figure 2.

Worldwide confirmed cases of BSE as of May 2007. Adapted from http:/www.oie.int./eng/info/en_esbmonde.htm.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
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Image of Figure 3.
Figure 3.

Schematic of migration patterns of abnormal prion protein reported in cases of typical BSE (T), atypical BSE (A or light and A or heavy) and scrapie. A has been reported in Japan, Italy, and Belgium, and A in France, the United Kingdom, and the United States.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
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Table 1.

Overview of prion protein properties

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22

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