Journal Article (Review Article)

DZNE-2023-00033

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Role of different recombinant PrP substrates in the diagnostic accuracy of the CSF RT-QuIC assay in Creutzfeldt-Jakob disease.

Silva-Correia, S. (First author)DZNE* ; Schmitz, M.DZNE* ; Fischer, A.DZNE* ; Hermann, P.DZNE* ; Zerr, I. (Last author)DZNE*

2023
Springer Heidelberg

This record in other databases:    

Please use a persistent id in citations: doi:10.1007/s00441-022-03715-9

Abstract: The development of the real-time quaking-induced conversion (RT-QuIC), an in vitro protein misfolding amplification assay, was an innovation in the scientific field of protein misfolding diseases. In prion diseases, these types of assays imitate the pathological conversion of the cellular prion protein (PrPC) into a protease-resistant and/or amyloid form of PrP, called PrP resistant (PrPRes). The RT-QuIC is an automatic assay system based on real-time measuring of thioflavin-T (Th-T) incorporation into amyloid fibrils using shaking for disaggregation. It has already been applied in diagnostics, drug pre-screening, and to distinguish between different prion strains. The seeded conversion efficiency and the diagnostic accuracy of the RT-QuIC assay strongly depend on the kind of recombinant PrP (rec PrP) substrate. The DNA sequences of different substrates may originate from different species, such as human, bank vole, and hamster, or from a combination of two species, e.g., hamster-sheep chimera. In routine use, either full-length (FL) or truncated substrates are applied which can accelerate the conversion reaction, e.g., to a more sensitive version of RT-QuIC assay. In the present review, we provide an overview on the different types of PrP substrates (FL and truncated forms), recapitulate the production and purification process of different rec PrP substrates, and discuss the diagnostic value of CSF RT-QuIC in human prion disease diagnostics.

Keyword(s): Cricetinae (MeSH) ; Humans (MeSH) ; Animals (MeSH) ; Sheep (MeSH) ; Creutzfeldt-Jakob Syndrome: diagnosis (MeSH) ; Prions: metabolism (MeSH) ; Prion Proteins: metabolism (MeSH) ; Prions ; Creutzfeldt-Jakob disease ; Diagnostics ; Real-time quaking-induced conversion ; Recombinant prion protein substrates ; Prion Proteins

---

Contributing Institute(s):

1. Translational Studies and Biomarkers (AG Zerr)
2. Ext UMG Zerr (Ext UMG Zerr)
3. Epigenetics and Systems Medicine in Neurodegenerative Diseases (AG Fischer 1 ; AG Fischer)
4. Clinical Dementia Research Göttingen (Clinical Dementia Research Göttingen)

Research Program(s):

1. 353 - Clinical and Health Care Research (POF4-353) (POF4-353)
2. 352 - Disease Mechanisms (POF4-352) (POF4-352)

Appears in the scientific report 2023

---

Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Springer ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection ; Zoological Record

---