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Prion diseases are associated with the conformational conversion of the cellular prion protein (PrP C ) into the pathological scrapie isoform (PrP Sc ) in the brain. Both the  in vivo  and  in vitro  conversion of PrP C  into PrP Sc  is significantly inhibited by differences in amino acid sequence between the two molecules. Using protein misfolding cyclic amplification (PMCA), we now report that the recombinant full-length human PrP (rHuPrP23-231) (that is unglycosylated and lacks the glycophosphatidylinositol anchor) is a strong inhibitor of human prion propagation. Furthermore, rHuPrP23-231 also inhibits mouse prion propagation in a scrapie-infected mouse cell line. Notably, it binds to PrP Sc , but not PrP C , suggesting that the inhibitory effect of recombinant PrP results from blocking the interaction of brain PrP C  with PrP Sc . Our findings suggest a new avenue for treating prion diseases, in which a patient's own unglycosylated and anchorless PrP is used to inhibit PrP Sc  propagation without inducing immune response side effects.

Recombinant Human Prion Protein Inhibits Prion Propagation in vitro