NR AXTP
AU Nilsson,K.P.R.; Sigurdson,C.J.; Fransson,S.; Manco,G.; Hammarström,P.; Aguzzi,A.
TI Luminescent Conjugated Polymers - Conformation Sensitive Optical Probes for Staining and Characterization of Prion Strains
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Natural and Experimental Strains P02.19
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB
Several questions still remain regarding the molecular mechanism of protein aggregation and the information encoded in the disease associated multiple conformations and morphologies of the protein deposits. For instance, the prion strain phenomenon is believed to be associated with distinct tertiary and/or quaternary structure of the prion aggregates.
Here we report that histochemical LCP stains yield a simple and sensitive method for characterization of native prion aggregates having distinct biochemical and
histopathological properties, indicative of specific prion strain isolates. LCPs reliably distinguished a variety of prion protein aggregates, including mouse-passaged prion strains of bovine spongiform encephalopathy (mBSE), sheep scrapie (mPSS), chronic wasting disease (mCWD) and the Rocky Mountain Laboratory (RML) prion strain. LCPs stained all amyloidogenic prion deposits identified by ThT and Congo red. In addition, an anionic LCP, PTAA, being bound to congophilic mCWD, mBSE or mPSS plaques emitted light with different colors. Hence, the emission from an individual LCP can be used to distinguish congophilic aggregates, formally classified as amyloid, arising in individual murine prion isolates. LCPs also stained diffuse non-congophilic prion aggregates and by using two LCPs with distinct ionic-side chain functionalities, a difference in the stainability pattern of the LCPs was observed. Each of the prion isolates being used display unique signatures in a variety of biochemical and histopathological parameters, suggesting that each isolate represents a unique prion strain. Therefore, the photophysical phenomena revealed by the emission spectra of PTAA or the stainability difference seen for LCPs with distinct ionic side-chain
functionalities are most likely strain specific. The technique is also demonstrated for natural prion diseases, such as sporadic CJD, BSE, atyptical BSE (BASE), scrapie and CWD.
AD K.P.R. Nilsson, C.J. Sigurdson, S. Fransson, G. Manco, A. Aguzzi, UniversitätsSpital Zürich, Institute for Neuropathology, Switzerland; Per Hammarström, University of Linköping, Department of Chemistry, Sweden
SP englisch
PO Schottland