title: Glycosylation and misfolding of PrP.
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.
authors.affiliation: Neuropathogenesis Unit, Institute for Animal Health, Ogston Building, Edinburgh EH9 3JF, UK. frances.wiseman@bbsrc.ac.uk
authors.forename: F
authors.initials: F
authors.lastname: Wiseman
authors.forename: E
authors.initials: E
authors.lastname: Cancellotti
authors.forename: J
authors.initials: J
authors.lastname: Manson
mesh_terms: D000818:Animals; D004195:Disease Models, Animal; D018014:Gene Transfer Techniques; D006031:Glycosylation; D051379:Mice; D017354:Point Mutation; D011328:Prions / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D011328:Prions; D011994:Recombinant Proteins