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Background and Purpose Te level of 14-3-3 protein in the cerebrospinal fuid (CSF) is increased in Creutzfeldt-Jakob disease (CJD) patients, which has led to it being used as a clinical biomarker for the ante-mortem diagnosis of human prion diseases. However, the specifcity of the 14-3-3 protein is less reliable for CJD diagnosis. Newly developed assays including real-time quaking-induced conversion (RT-QuIC) have made it possible to detect the PrPSc-like abnormal prion isoform with a high sensitivity in animal and human specimens that might contain a minute amount of PrPScdue to in vitro prion replication. MethodszzTis study applied a highly sensitive RT-QuIC assay using recombinant human PrP to detect PrPScin the CSF of 81 patients with sporadic CJD (sCJD) in Korea. ResultszzRT-QuIC analysis of the CSF samples based on the expression levels of 14-3-3 and total tau proteins revealed positivity in 62 of 81 sCJD patients (sensitivity of 76.5%) but no positive results in the 100 non-CJD patients. Conclusions Te sensitivity of the RT-QuIC in this study was similar to that in some previous reports, and the specifcity of RT-QuIC was higher than that of 14-3-3 in CSF, suggesting that RT-QuIC analysis can complement the weakness of the specifcity of 14-3-3 for the diagnosis of sCJD. Tese results indicate that RT-QuIC might be very useful for the rapid and specifc diagnosis of sCJD and provide a practical novel method for the ante-mortem diagnosis of human prion diseases.

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