Biochemical and strain properties of CJD prions: complexity versus simplicity
Article first published online: 20 SEP 2011
© 2011 The Authors. Journal of Neurochemistry © 2011 International Society for Neurochemistry
Journal of Neurochemistry
Volume 119, Issue 2, pages 251–261, October 2011
How to Cite
Haïk, S. and Brandel, J.-P. (2011), Biochemical and strain properties of CJD prions: complexity versus simplicity. Journal of Neurochemistry, 119: 251–261. doi: 10.1111/j.1471-4159.2011.07399.x
- Issue published online: 5 OCT 2011
- Article first published online: 20 SEP 2011
- Accepted manuscript online: 25 JUL 2011 09:53AM EST
- Received May 27, 2011; revised manuscript received July 20, 2011; accepted July 20, 2011.
- transmissible spongiform encephalopathy
J. Neurochem. (2011) 119, 251–261.
Prions, the agents responsible for transmissible spongiform encephalopathies, are infectious proteins consisting primarily of scrapie prion protein (PrPSc), a misfolded, β-sheet enriched and aggregated form of the host-encoded cellular prion protein (PrPC). Their propagation is based on an autocatalytic PrP conversion process. Despite the lack of a nucleic acid genome, different prion strains have been isolated from animal diseases. Increasing evidence supports the view that strain-specific properties may be enciphered within conformational variations of PrPSc. In humans, sporadic Creutzfeldt-Jakob disease (sCJD) is the most frequent form of prion diseases and has demonstrated a wide phenotypic and molecular spectrum. In contrast, variant Creutzfeldt-Jakob disease (vCJD), which results from oral exposure to the agent of bovine spongiform encephalopathy, is a highly stereotyped disease, that, until now, has only occurred in patients who are methionine homozygous at codon 129 of the PrP gene. Recent research has provided consistent evidence of strain diversity in sCJD and also, unexpectedly enough, in vCJD. Here, we discuss the puzzling biochemical/pathological diversity of human prion disorders and the relationship of that diversity to the biological properties of the agent as demonstrated by strain typing in experimental models.