The finding that a common blood protein sticks to rogue prions but ignores the normal, harmless variety could one day form the basis of a test for prion diseases such as BSE and CJD. As well as offering insight into how prions cause disease, this selective binding activity might be harnessed to sweep blood products free of infection.
Adriano Aguzzi of the University Hospital of Zurich and colleagues use the protein ‘plasminogen’ harvested from human and mouse blood serum [Nature, Vol. 408, No. 6811, 23 November 2000, pp. 479–483]. They coat tiny magnetic beads with the sticky protein and mix them with samples of brain tissue from mice infected with the sheep prion disease scrapie. The team find that the beads bind the infectious prions that cause scrapie (PrPSc) but not similar, non-infectious prions (PrPC). The beads also selectively retrieve the prions that cause CJD from the brain tissue of human sufferers.
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