NR AOVG
AU Kuhn,F.; Pürro,M.; Zwald,D.; Schmid,J.; Biffiger,K.; Mehl,M.; Miglino,N.; Fischer,K.; Oesch,B.; Raeber,A.J.
TI Towards a Live Test for Prion Diseases
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - DG-54
PT Konferenz-Poster
AB There is an urgent need to develop sensitive assays based on blood or urine for ante mortem diagnosis of transmissible spongiform encephalopathies (TSE). Because the concentration of the pathological prion protein (PrPsc) in peripheral body fluids is 100 to 1000-fold lower than in the central nervous system, methods to enrich for PrPsc in these tissues are of paramount importance. Furthermore PrPsc in body fluids might show different biochemical properties than brain PrPsc such as protease resistance or aggregation. We have developed an immunochemical assay using the antibody 15B3 (Korth et al., Nature, 390:74-77) which specifically recognizes the pathological isoform of the prion protein, PrPsc, from different species such as human, bovine, deer, mouse and sheep. In contrast to currently used TSE tests which use protease digestion to distinguish between PrPc and PrPsc, the antibody 15B3 enables us to omit proteolysis in the test procedure. Therefore, the test is not only shortened and simplified but more importantly the risk of missing protease sensitive PrPsc is reduced. With this test protocol, we are able to detect PrPsc from brain homogenates spiked into total blood samples that contain a vast excess of PrPc. Furthermore the antibody 15B3 is able to discriminate between different PrPsc conformers from sporadic and variant CJD cases suggesting that a 15B3-based diagnostic test could be used in assessing the risk of vCJD prions in blood and blood-derived products.
AD Franziska Kuhn, Mario Pürro, Daniel Zwald, Jacqueline Schmid, Karin Biffiger, Martin Mehl, Nicola Miglino, Karin Fischer, Bruno Oesch, Alex J. Raeber, Prionics AG, Switzerland
SP englisch
PO Deutschland