NR AUOZ
AU Wiseman,F.; Cancellotti,E.; Manson,J.
TI Glycosylation and misfolding of PrP
QU Biochemical Society Transactions 2005 Nov; 33(5): 1094-5
PT journal article
AB 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.
MH Animals; Disease Models, Animal; Gene Transfer Techniques; *Glycosylation; Mice; Point Mutation; Prions/genetics/*metabolism; Recombinant Proteins/metabolism; Research Support, Non-U.S. Gov't
AD Neuropathogenesis Unit, Institute for Animal Health, Ogston Building, Edinburgh EH9 3JF, UK. frances.wiseman@bbsrc.ac.uk
SP englisch
PO England