NEW YORK (Reuters Health) - Researchers have identified a human prion protein that appears to prevent expression of variant Creutzfield-Jakob disease (CJD). As such, individuals with a certain genotype may be relatively resistant to the human form of bovine spongiform encephalopathy (BSE).
Using transgenic mice, Dr. John Collinge, from University College London, and colleagues found that for a BSE phenotype to occur, a particular form of human prion protein was needed. Specifically, methionine was required at residue 129 of the protein.
In contrast, if valine was at residue 129 instead, BSE-derived prions were unable to be transmitted and a distinct non-BSE phenotype appeared, according to the report in the November 11th online issue of Sciencexpress.
With prion protein featuring a polymorphic residue 129, propagation of distinct prion strains was noted after infection with BSE prion, the investigators state.
“We have demonstrated that BSE and variant CJD prion infection in transgenic mice can result in the propagation of distinct molecular and neuropathological phenotypes dependent upon host prion protein residue 129 and possibly other, as yet unidentified, disease modifying loci,” Dr. Collinge’s team concludes.
Source: Sciencexpress 2004. [ Google search on this article ]
MeSH Headings:Animal Diseases: Biological Sciences: Biology: Disease Models, Animal: Genetics: Genetics, Microbial: Polymorphism, Single Nucleotide: Biological Sciences: DiseasesCopyright © 2002 Reuters Limited. All rights reserved. Republication or redistribution of Reuters content, including by framing or similar means, is expressly prohibited without the prior written consent of Reuters. Reuters shall not be liable for any errors or delays in the content, or for any actions taken in reliance thereon. Reuters and the Reuters sphere logo are registered trademarks and trademarks of the Reuters group of companies around the world.
