Journal
FEBS LETTERS
Volume 583, Issue 22, Pages 3671-3675Publisher
WILEY
DOI: 10.1016/j.febslet.2009.10.049
Keywords
Transmissible spongiform encephalopathy; Prion; Prion protein; Conformational conversion; Glycophosphatidylinositol anchor
Funding
- National Institutes of Health [NS44158, AG14359]
Ask authors/readers for more resources
Transmissible spongiform encephalopathies are associated with an autocatalytic conversion of normal prion protein, PrPC, to a protease-resistant form, PrPres. This autocatalytic reaction can be reproduced in vitro using a procedure called protein misfolding cyclic amplification (PMCA). Here we show that, unlike brain-derived PrPC, bacterially-expressed recombinant prion protein (rPrP) is a poor substrate for PrPres amplification in a standard PMCA reaction. The differences between PrPC and rPrP appear to be due to the lack of the glycophosphatidylinositol anchor in the recombinant protein. These findings shed a new light on prion protein conversion process and have important implications for the efforts to generate synthetic prions for structural and biophysical studies. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available