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Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions.
- Source :
- Cellular & Molecular Life Sciences; Feb2008, Vol. 65 Issue 4, p631-643, 13p, 3 Black and White Photographs, 1 Diagram, 1 Graph
- Publication Year :
- 2008
-
Abstract
- Human prion diseases are characterized by the accumulation in the brain of proteinase K (PK)-resistant prion protein designated PrP27 – 30 detectable by the 3F4 antibody against human PrP109 – 112. We recently identified a new PK-resistant PrP species, designated PrP<superscript>*20</superscript>, in uninfected human and animal brains. It was preferentially detected with the 1E4 antibody against human PrP 97 – 108 but not with the anti-PrP 3F4 antibody, although the 3F4 epitope is adjacent to the 1E4 epitope in the PrP<superscript>*20</superscript> molecule. The present study reveals that removal of the N-terminal amino acids up to residue 91 significantly increases accessibility of the 1E4 antibody to PrP of brains and cultured cells. In contrast to cells expressing wild-type PrP, cells expressing pathogenic mutant PrP accumulate not only PrP<superscript>*20</superscript> but also a small amount of 3F4-detected PK-resistant PrP27 – 30. Remarkably, during the course of human prion disease, a transition from an increase in 1E4-detected PrP<superscript>*20</superscript> to the occurrence of the 3F4-detected PrP27 – 30 was observed. Our study suggests that an increase in the level of PrP<superscript>*20</superscript> characterizes the early stages of prion diseases. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 1420682X
- Volume :
- 65
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Cellular & Molecular Life Sciences
- Publication Type :
- Academic Journal
- Accession number :
- 30048433
- Full Text :
- https://doi.org/10.1007/s00018-007-7478-z