The real-Time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases

M Schmitz; M Cramm; F Llorens; D Müller-Cramm; S Collins; R Atarashi; K Satoh; CD Orrù; BR Groveman; S Zafar; WJ Schulz-Schaeffer; B Caughey; I Zerr

Journal article

The real-Time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases

M Schmitz, M Cramm, F Llorens, D Müller-Cramm, S Collins, R Atarashi, K Satoh, CD Orrù, BR Groveman, S Zafar, WJ Schulz-Schaeffer, B Caughey, I Zerr

Nature Protocols | NATURE PUBLISHING GROUP | Published : 2016

DOI: 10.1038/nprot.2016.120

Abstract

The development and adaption of in vitro misfolded protein amplification systems has been a major innovation in the detection of abnormally folded prion protein scrapie (PrP Sc) in human brain and cerebrospinal fluid (CSF) samples. Herein, we describe a fast and efficient protein amplification technique, real-Time quaking-induced conversion (RT-QuIC), for the detection of a PrP Sc seed in human brain and CSF. In contrast to other in vitro misfolded protein amplification assays-such as protein misfolding cyclic amplification (PMCA)-which are based on sonication, the RT-QuIC technique is based on prion seed-induced misfolding and aggregation of recombinant prion protein substrate, accelerated ..

View full abstract

University of Melbourne Researchers

Steven Collins Author

Related Projects (1)

DETERMINING NORMAL PRION PROTEIN FUNCTION, EMPHASISING THE ROLE PLAYED BY PROTEIN CLEAVAGE, AND ALSO DEFINING THE RELATIONSHIP BETWEEN SURVEILLANCE INTENSITY AND ANNUAL SPORADIC CJD INCIDENCE

As a neurologist undertaking research into prion diseases over an extended period, I have been able to lead and participate in many projects..

Grants

Awarded by Japan Society for the Promotion of Science

Funding Acknowledgements

This study was performed as part of the Clinical Dementia Center at the University Medical Center Gottingen and was partly supported by grants from the EU Joint Program-Neurodegenerative Disease Research (JPND-DEMTEST (Biomarker-based diagnosis of rapid progressive dementias-optimization of diagnostic protocols, 01ED1201A) and by the Robert Koch Institute through funds from the Federal Ministry of Health (grant no. 1369341). This work was also supported in part by the Intramural Research Program of the NIAID. S.C. is supported by a NHMRC Practitioner Fellowship (identification no. APP1005816) and by the Australian National Creutzfeldt-Jakob Disease Registry (ANCJDR), which is funded by the Commonwealth Department of Health.