1. Nat. Rev. Neurol. doi:10.1038/nrneurol.2016.65
Figure 1 Tissue and body fluid samples for prion protein detection in patients with CJD
Figure 1 | Tissue and body fluid samples for prion protein detection in patients with CJD. Diagnosis of the different forms of Creutzfeldt–Jakob disease (CJD) requires samples from different tissues. In genetic CJD, DNA sequencing of blood samples detects prion protein gene (PRNP) mutations or insertions. In sporadic CJD, CJD-specific misfolded prion protein (PrPCJD) detected in the brain biopsy samples provides a definitive diagnosis of the disease. Real-time quaking-induced conversion (RT-QuIC) assay of the cerebrospinal fluid (CSF) and olfactory mucosa can demonstrate the presence of PrPCJD with a sensitivity and specificity of nearly 100%. In peripheral tissues, PrPCJD has occasionally been detected postmortem in muscle, spleen and lymph nodes by immunoblotting and/or immunohistochemistry. In variant CJD, PrPCJD can be detected in tonsil biopsies by immunoblotting and/or immunohistochemistry, and in blood and urine by ELISA and protein misfolding cyclic amplification (PMCA). Postmortem, PrPCJD has also been detected in muscle and lymporeticular tissues. *PrPCJD detected from postmortem samples by immunohistochemistry and immunoblotting.
Zanusso, G. et al. (2016) Advanced tests for early and accurate diagnosis of Creutzfeldt–Jakob disease
Nat. Rev. Neurol. doi: /nrneurol