Abstract
The TSEs (transmissible spongiform encephalopathies) are not only devastating neurological diseases but also provide a biochemical conundrum; how can a disease agent replicate in the apparent absence of genetic material? The prion hypothesis proposes that the TSE agent is a misfolded form of the host glycoprotein PrP (prion protein). However, a number of questions regarding the hypothesis remain to be addressed. We are using gene-targeted PrP transgenics models to investigate these issues. Here we discuss our recent results that examine the importance of PrP's N-glycans to the misfolding of the protein.
Original language | English |
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Pages (from-to) | 1094-5 |
Number of pages | 2 |
Journal | Biochemical Society Transactions |
Volume | 33 |
Issue number | Pt 5 |
DOIs | |
Publication status | Published - Nov 2005 |
Keywords
- Animals
- Disease Models, Animal
- Gene Transfer Techniques
- Glycosylation
- Mice
- Point Mutation
- Prions
- Recombinant Proteins