Surface plasmon resonance was used to develop a rapid, label-free and sensitive immunoassay for detection of Prion protein (PrP). Anti-PrP monoclonal antibodies immobilized on the biosensor surface were allowed to bind various concentrations of cellular prion protein (PrP C ), followed by a pulse with additional soluble anti-PrP polyclonal antibodies to intensify the signal. The interaction of antibody with antigen was monitored in real time. With this method, it was possible to detect PrP C with a limit of 31.7 ng/ml in serum and 13.1 ng/ml in HEPES-saline, requiring 1 h for a single sample measurement. The assay also detected misfolded prion protein (PrP Sc ) in spiked serum and PrP Sc in scrapie-infected mouse brains. This is a rapid and sensitive assay for the detection of PrP in serum that could be developed into a platform for a serum-based TSE test.
Archives of Virology – Springer Journals
Published: Dec 1, 2009
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