Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions
Identifieur interne : 001624 ( Main/Exploration ); précédent : 001623; suivant : 001625Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions
Auteurs : J. Yuan [États-Unis] ; Z. Dong [États-Unis] ; J.-P. Guo [Canada] ; J. Mcgeehan [Royaume-Uni] ; X. Xiao [États-Unis] ; J. Wang [États-Unis] ; I. Cali [États-Unis] ; P. L. Mcgeer [Canada] ; N. R. Cashman [Canada] ; R. Bessen [États-Unis] ; W. K. Surewicz [États-Unis] ; G. Kneale [Royaume-Uni] ; R. B. Petersen [États-Unis] ; P. Gambetti [États-Unis] ; W. Q. Zou [États-Unis]Source :
- Cellular and Molecular Life Sciences [ 1420-682X ] ; 2008-02-01.
English descriptors
- KwdEn :
Abstract
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*20, 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*20 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*20 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*20 to the occurrence of the 3F4-detected PrP27-30 was observed. Our study suggests that an increase in the level of PrP*20 characterizes the early stages of prion diseases.
Url:
DOI: 10.1007/s00018-007-7478-z
Affiliations:
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<front><div type="abstract" xml:lang="en">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*20, 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*20 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*20 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*20 to the occurrence of the 3F4-detected PrP27-30 was observed. Our study suggests that an increase in the level of PrP*20 characterizes the early stages of prion diseases.</div>
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