Glycosylation and misfolding of PrP

F Wiseman, E Cancellotti, J Manson

Research output: Contribution to journalArticlepeer-review


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 languageEnglish
Pages (from-to)1094-5
Number of pages2
JournalBiochemical Society Transactions
Issue numberPt 5
Publication statusPublished - Nov 2005


  • Animals
  • Disease Models, Animal
  • Gene Transfer Techniques
  • Glycosylation
  • Mice
  • Point Mutation
  • Prions
  • Recombinant Proteins


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