NR AOZW
AU Trieschmann,L.; Kaschig,K.; Schaupp,M.; Navarrete Santos,A.
TI Highly sensitive detection of prion protein fibrils by FACS-analysis
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - DG-09
PT Konferenz-Poster
AB Depositions of abnormal proteins in the central nervous system are a hallmark of several neurodegenerative diseases, including Alzheimer's disease and prion diseases such as BSE and Creutzfeldt-Jakob disease. In prion diseases, the pathogen is a misfolded form (PrPsc) of the cellular prion protein, PrPc. PrPsc propagates by inducing PrPc to adopt its own pathological structure. In contrast to its normally folded counterpart, PrPsc is rich in ß-sheet structure and has a propensity to polymerize, forming large fibrillar aggregates. Here we present a method for detecting prion protein fibrils in vitro that takes advantage of the fibrillogenic properties of PrPsc and may become useful as a novel approach to the diagnosis of prion diseases. In vitro generated prion protein fibrils are elongated by the addition of recombinant PrP monomers tagged with a fluorescent dye. The resulting labelled fibrils are detected by flow cytometry. The method is robust and highly sensitive, allowing the detection of extremely low concentrations of fibrils down to the picomolar range.
AD L. Trieschmann, K. Kaschig, M. Schaupp, A. Navarrete Santos, ACGT ProGenomics AG, Halle (Saale), Germany
SP englisch
PO Deutschland