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KMID : 1130620160120010101
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Journal of Clinical Neurology
2016 Volume.12 No. 1 p.101 ~ p.106
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Real-Time Quaking-Induced Conversion Analysis for the Diagnosis of Sporadic Creutzfeldt-Jakob Disease in Korea
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Park Jeong-Ho
Choi Yeong-Gon
Park Seok-Joo
Choi Hong-Seok
Choi Kyung-Chan
Choi Eun-Kyoung
Kim Yong-Sun
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Abstract
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Background and Purpose: The level of 14-3-3 protein in the cerebrospinal fluid (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 specificity 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 PrPSc due to in vitro prion replication.
Methods: This study applied a highly sensitive RT-QuIC assay using recombinant human PrP to detect PrPSc in the CSF of 81 patients with sporadic CJD (sCJD) in Korea.
Results: RT-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: The sensitivity of the RT-QuIC in this study was similar to that in some previous reports, and the specificity of RT-QuIC was higher than that of 14-3-3 in CSF, suggesting that RT-QuIC analysis can complement the weakness of the specificity of 14-3-3 for the diagnosis of sCJD. These results indicate that RT-QuIC might be very useful for the rapid and specific diagnosis of sCJD and provide a practical novel method for the ante-mortem diagnosis of human prion diseases.
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KEYWORD
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Creutzfeldt-Jakob disease, cerebrospinal fluid, RT-QuIC, 14-3-3, total tau protein
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