Back to Search
Start Over
Discriminating Scrapie and Bovine Spongiform Encephalopathy Isolates by Infrared Spectroscopy of Pathological Prion Protein
- Source :
- Journal of Biological Chemistry. 279:33847-33854
- Publication Year :
- 2004
- Publisher :
- Elsevier BV, 2004.
-
Abstract
- For the surveillance of transmissible spongiform encephalopathies (TSEs) in animals and humans, the discrimination of different TSE strains causing scrapie, BSE, or Creutzfeldt-Jakob disease constitutes a substantial challenge. We addressed this problem by Fourier transform-infrared (FT-IR) spectroscopy of pathological prion protein PrP27-30. Different isolates of hamster-adapted scrapie (263K, 22A-H, and ME7-H) and BSE (BSE-H) were passaged in Syrian hamsters. Two of these agents, 22A-H and ME7-H, caused TSEs with indistinguishable clinical symptoms, neuropathological changes, and electrophoretic mobilities and glycosylation patterns of PrP27-30. However, FT-IR spectroscopy revealed that PrP27-30 of all four isolates featured different characteristics in the secondary structure, allowing a clear distinction between the passaged TSE agents. FT-IR analysis showed that phenotypic information is mirrored in beta-sheet and other secondary structure elements of PrP27-30, also in cases where immunobiochemical typing failed to detect structural differences. If the findings of this study hold true for nonexperimental TSEs in animals and humans, FT-IR characterization of PrP27-30 may provide a versatile tool for molecular strain typing without antibodies and without restrictions to specific TSEs or mammalian species.
- Subjects :
- PrPSc Proteins
animal diseases
Bovine spongiform encephalopathy
Scrapie
Biology
Biochemistry
Protein Structure, Secondary
Cricetinae
Spectroscopy, Fourier Transform Infrared
medicine
Animals
Tissue Distribution
Typing
Prion protein
Molecular Biology
Pathological
Brain Chemistry
Mesocricetus
Strain typing
Cell Biology
medicine.disease
Phenotype
Virology
PrP 27-30 Protein
nervous system diseases
Encephalopathy, Bovine Spongiform
Disease Models, Animal
biology.protein
Cattle
Endopeptidase K
Antibody
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 279
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....2bc4524df755ce3f7ff3c8f59e0d26a6