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Listen to this siteMonday 30 June 2008
Study Duration : November 2007 to October 2010
Contractor : Heinriche-Heine-University of Duesseldorf
The pathological isoform of the prion protein (PrP Sc ) can be considered to be an early biomarker for transmissible spongiform encephalopathy (TSE) infection such as scrapie in sheep or BSE in cattle. PrP Sc is composed of a proteinase K (PK) resistant (resPrP Sc ) and PK-sensitive portion. The non-pathogenic, cellular isoform, PrPC, is also sensitive to PK-digestion. Most TSE-diagnostic approaches today are based on the detection of the resPrP Sc -portion only, however this research will investigate the aggregated PrP Sc structure as a specific marker, not depending upon PK resistance
A new method has been developed in which PrP Sc -particles, the PK-sensitive as well as the PK-resistant portion, are bound to a surface via capture antibodies. The PrP Sc -particles are labelled with two different antibodies carrying different fluorescent labels. The labelled PrP Sc -particles are evaluated using Fluorescence Intensity Distribution Analysis (FIDA) which captures fluorescence from the two different antibodies. To enhance sensitivity a prion protein amplification (PPA) method will be used which in combination with surface-FIDA should result in an ultra sensitive detection method for TSE-associated particles. This could aid the detection of low levels of PrPSc in the early state of disease and in non-central nervous system tissues or body fluids. The research aims to optimise surface-FIDA in respect to sensitivity and specificity of detecting single PrP Sc -particles. Body fluids such as blood will be used to investigate the application of surface-FIDA to living animals. Brain tissue and CSF from preclinical animals will also be used to investigate the very early state of disease.
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