Glycosylation and misfolding of PrP. (26th October 2005)

• Record Type: Journal Article
• Authors: Wiseman, F.; Cancellotti, E.; Manson, J.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 5(2005)
• Page Start: 1094
• Page End: 1095
• Publication Date: 2005-10-26
• Subjects: Creutzfeldt–Jacob disease (CJD) -- glycosylation -- prion -- protein folding -- PrP -- transmissible spongiform encephalopathy (TSE); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0331094
• Languages: English
• ISSNs: 0300-5127

Abstract

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.