Mok, TH; Nihat, A; Luk, C; Sequeira, D; Batchelor, M; Mead, S; Collinge, J; Mok, TH; Nihat, A; Luk, C; Sequeira, D; Batchelor, M; Mead, S; Collinge, J; Jackson, GS; - view fewer (2021) Bank vole prion protein extends the use of RT-QuIC assays to detect prions in a range of inherited prion diseases. Scientific Reports , 11 (1) , Article 5231. 10.1038/s41598-021-84527-9.

Preview

Text Mead_Bank vole prion protein extends the use of RT-QuIC assays to detect prions in a range of inherited prion diseases_VoR.pdf - Published Version Download (3MB) | Preview

Abstract

The cerebrospinal fluid (CSF) real-time quaking-induced conversion assay (RT-QuIC) is an ultrasensitive prion amyloid seeding assay for diagnosis of sporadic Creutzfeldt-Jakob disease (CJD) but several prion strains remain unexplored or resistant to conversion with commonly used recombinant prion protein (rPrP) substrates. Here, bank vole (BV) rPrP was used to study seeding by a wide range of archived post-mortem human CSF samples from cases of sporadic, acquired and various inherited prion diseases in high throughput 384-well format. BV rPrP substrate yielded positive reactions in 70/79 cases of sporadic CJD [Sensitivity 88.6% (95% CI 79.5-94.7%)], 1/2 variant CJD samples, and 9/20 samples from various inherited prion diseases; 5/57 non-prion disease control CSFs had positive reactions, yielding an overall specificity of 91.2% (95% CI 80.1-97.1%). Despite limitations of using post-mortem samples and our results' discrepancy with other studies, we demonstrated for the first time that BV rPrP is susceptible to conversion by human CSF samples containing certain prion strains not previously responsive in conventional rPrPs, thus justifying further optimisation for wider diagnostic and prognostic use.

Download activity - last month

Export as JSONXMLCSV

Download activity - last 12 months

Export as JSONXMLCSV

Downloads by country - last 12 months

Export as CSVXMLJSON

Archive Staff Only

View Item