Javascript must be enabled for the correct page display

Prion propagation principles

Voshart, D.C. (2017) Prion propagation principles. Master's Thesis / Essay, Biomedical Sciences.

MasterLS_BMS_2017_DCVoshart.pdf - Published Version

Download (893kB) | Preview
[img] Text
Toestemming.pdf - Other
Restricted to Backend only

Download (82kB)


Transmissible spongiform encephalitis (TSE) are a group of currently incurable, fatal diseases Unlike any other disease, TSE’s can be induced on a genetic, spontaneous or infectious base. It is generally assumed that TSE’s are caused by misfolded prion protein. However, this was, and is still, opposed. Furthermore, the exact mechanism of prion infectivity, prion propagation, is still debated. Therefore, the aim of this essay was to compare theories of prion propagation. First, an historical overview of the slow virus and infectious protein theories was given. Overwhelming evidence shows that TSE’s are indeed caused by an infectious protein instead of a virus. Second, theories of prion protein misfolding and aggregate formation were discussed. Nucleation-dependent polymerization is the best fitting model for prion protein misfolding and amyloid formation. Third, the protein X and protein-only theory were discussed. Here, the question if co-factors were necessary for prion-propagation was most important. Co-factors were considered to very important, but not essential, for prion propagation. Therefore, the protein X theory was dismissed. These insights can help develop treatment strategies for TSE’s.

Item Type: Thesis (Master's Thesis / Essay)
Degree programme: Biomedical Sciences
Thesis type: Master's Thesis / Essay
Language: English
Date Deposited: 15 Feb 2018 08:32
Last Modified: 15 Feb 2018 08:32

Actions (login required)

View Item View Item