Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 407773
Title Human Variant Creutzfeldt-Jakob disease and sheep scrapie PrP (res) detection using seeded conversion of recombinant prion protein.
Author(s) Orrú, C.D.; Wilham, J.M.; Hughson, A.G.; Raymond, L.D.; McNally, K.L.; Bossers, A.; Ligios, C.; Caughey, B.
Source Protein Engineering, Design & Selection 22 (2009)8. - ISSN 1741-0126 - p. 515 - 521.
DOI http://dx.doi.org/10.1093/protein/gzp031
Department(s) CVI Infection Biology
Publication type Refereed Article in a scientific journal
Publication year 2009
Keyword(s) in-vitro amplification - misfolding cyclic amplification - cell-free formation - resistant state - ultrasensitive detection - cerebrospinal-fluid - prpsc - brain - form - binding
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.
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