The diagnostic utility of real-time quaking-induced conversion assay (RT-QuIC) in the diagnosis of sporadic Creutzfeldt-Jakob disease
6th Clinical Microbiology Conference
October 20-22, 2016 Rome, Italy

Alison J E Green

University of Edinburgh, UK

Posters & Accepted Abstracts: Clin Microbiol

Abstract:

Sporadic Creutzfeldt-Jakob disease (sCJD) belongs to a family of fatal neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs) or prion diseases. Neuropathologically these diseases are characterized by the posttranslational conformational change of a normal cellular protein called prion protein (PrPC) into a disease-associated form, termed PrPSc. PrPSc is partially protease-resistant and can induce PrPC to undergo a conformational change and produce more PrPSc in a self-propagating manner by a seeded aggregation process. Current diagnostic criteria for sCJD rely on clinical features and the results of EEG, MRI and the presence of 14-3-3 in the cerebrospinal fluid (CSF). These tests are not specific for sCJD. A new approach to the pre-mortem diagnosis of sCJD has been to exploit the ability of small amounts of CSF PrPSc to convert native PrP into PrPSc in a newly described protein aggregation assay known as real-time quaking induced conversion (RT-QuIC). In 2012 we reported that a retrospective study showed that CSF RT-QuIC had a sensitivity of 89% and a specificity of 99% for sCJD. Results of a prospective audit of CSF RT-QuIC in the United Kingdom showing that it has a sensitivity of 90% and a specificity of 100% will be presented and the role of RT-QuIC in the clinical diagnosis of sCJD described.

Biography :

Email: Alison.Green@ed.ac.uk