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- Title
Human variant Creutzfeldt–Jakob disease and sheep scrapie PrPres detection using seeded conversion of recombinant prion protein.
- Authors
Orrú, Christina D.; Wilham, Jason M.; Hughson, Andrew G.; Raymond, Lynne D.; McNally, Kristin L.; Bossers, Alex; Ligios, Ciriaco; Caughey, Byron
- Abstract
The pathological isoform of the prion protein (PrPres) can serve as a marker for prion diseases, but more practical tests are needed for preclinical diagnosis and sensitive detection of many prion infections. Previously we showed that the quaking-induced conversion (QuIC) assay can detect sub-femtogram levels of PrPres in scrapie-infected hamster brain tissue and distinguish cerebral spinal fluid (CSF) samples from normal and scrapie-infected hamsters. We now report the adaptation of the QuIC reaction to prion diseases of medical and agricultural interest: human variant Creutzfeldt-Jakob disease (vCJD) and sheep scrapie. PrPres-positive and -negative brain homogenates from humans and sheep were discriminated within 1–2 days with a sensitivity of 10–100 fg PrPres. More importantly, in as little as 22 h we were able to distinguish CSF samples from scrapie-infected and uninfected sheep. These results suggest the presence of prions in CSF from scrapie-infected sheep. This new method enables the relatively rapid and sensitive detection of human CJD and sheep scrapie PrPres and may facilitate the development of practical preclinical diagnostic and high-throughput interference tests.
- Subjects
PRIONS; PROTEINS; PRION diseases; CREUTZFELDT-Jakob disease; SCRAPIE; VIRUS diseases in sheep
- Publication
PEDS: Protein Engineering, Design & Selection, 2009, Vol 22, Issue 8, p515
- ISSN
1741-0126
- Publication type
Article
- DOI
10.1093/protein/gzp031