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Detection of prion particles in samples of BSE and scrapie by fluorescence correlation spectroscopy without proteinase K digestion
- Source :
- Biological chemistry. 387(1)
- Publication Year :
- 2006
-
Abstract
- A characteristic feature of prion diseases such as bovine spongiform encephalopathy (BSE) is the accumulation of a pathological isoform of the host-encoded prion protein, PrP. In contrast to its cellular isoform PrP c , the pathological isoform PrP S c forms insoluble aggregates. All commercial BSE tests currently used for routine testing are based on the proteinase K (PK) resistance of PrP, but not all pathological PrP is PK-resistant. In the present study, single prion particles were counted by fluorescence correlation spectroscopy (FCS). The property of PK resistance is not required, i.e., both the PK-resistant and the PK-sensitive parts of the prion particles are detectable. PrP aggregates were prepared from the brains of BSE-infected cattle, as well as from scrapie-infected hamsters, by the NaPTA precipitation method without PK digestion. They were labeled using two different PrP-specific antibodies for FCS measurements in the dual-color mode (2D-FIDA). Within the limited number of samples tested, BSE-infected cattle and scrapie-infected hamsters in the clinical stage of the disease could be distinguished with 100% specificity from a control group. Thus, a diagnostic tool for BSE detection with complete avoidance of PK treatment is presented, which should have particular advantages for testing animals in the preclinical stage.
- Subjects :
- Gene isoform
Prions
animal diseases
Bovine spongiform encephalopathy
Clinical Biochemistry
Fluorescence correlation spectroscopy
Scrapie
Biology
Biochemistry
Cricetinae
medicine
Animals
Molecular Biology
Medulla Oblongata
medicine.disease
Proteinase K
Virology
Molecular biology
nervous system diseases
Encephalopathy, Bovine Spongiform
Spectrometry, Fluorescence
biology.protein
Cattle
Antibody
Endopeptidase K
Digestion
Preclinical stage
Subjects
Details
- ISSN :
- 14316730
- Volume :
- 387
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biological chemistry
- Accession number :
- edsair.doi.dedup.....5551f41d33c9144eae245111441dd3a2