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Review
. 2017 Oct;17(10):897-904.
doi: 10.1080/14737159.2017.1368389. Epub 2017 Sep 8.

Applications of the real-time quaking-induced conversion assay in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies

Niccolò Candelise  1 , Matthias Schmitz  1 , Susana Margarida Da Silva Correia  1 , Amandeep Singh Arora  1 , Anna Villar-Piqué  1 , Saima Zafar  1 , Franc Llorens  2 , Maria Cramm  1 , Inga Zerr  1
Affiliations
Review

Applications of the real-time quaking-induced conversion assay in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies

Niccolò Candelise et al. Expert Rev Mol Diagn. 2017 Oct.

Abstract

The development of in vitro protein misfolding amplification assays for the detection and analysis of abnormally folded proteins, such as proteinase K resistant prion protein (PrPres) was a major innovation in the prion field. In prion diseases, these types of assays imitate the pathological conversion of the cellular PrP (PrPC) into a proteinase resistant associated conformer or amyloid, called PrPres. Areas covered: The most prominent protein misfolding amplification assays are the protein misfolding cyclic amplification (PMCA), which is based on sonication and the real-time quaking-induced conversion (RT-QuIC) technique based on shaking. The more recently established RT-QuIC is fully automatic and enables the monitoring of misfolded protein aggregates in real-time by using a fluorescent dye. Expert commentary: RT-QuIC is a very robust and highly reproducible test system which is applicable in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies.

Keywords: Real-time quaking-induced conversion; aggregation; prion protein; protein misfolding; sporadic Creutzfeldt-Jakob disease.

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