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The molecular basis underlying the conversion of normal prion protein (PrP C ) into abnormal prion protein (PrP Sc ) has not been fully elucidated. The protein-misfolding cyclic amplification (PMCA) technique, which can amplify PrP Sc in vitro with the use of intermittent sonication, mimics the process of in vivo PrP Sc replication. Accumulating evidence suggests that co-factors other than PrP may play a crucial role in the faithful replication of PrP Sc . In conventional PMCA, brain homogenates (BHs) from normal animals are used as the PrP C substrate. Since BHs contain many impurities, it is difficult to identify the co-factors using conventional PMCA. Thus, we developed a modified PMCA system using baculovirus and insect cell-derived recombinant PrP as a substrate (insect cell PMCA; iPMCA). We demonstrated that nucleic acids and glycosaminoglycans (GAGs) such as heparan sulfate (HS) or its analogue heparin (HP) are critical for PrP Sc amplification in iPMCA. Of note, the addition of HS or HP restored the conversion efficiency in iPMCA under nucleic acid-depleted conditions. Moreover, the iPMCA products were infectious and preserved the strain properties of the input seed PrP Sc . These data suggest that not only nucleic acids but also some GAGs play an important role in facilitating faithful replication of prions, at least in vitro.

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Elucidation of the Molecular Basis of Abnormal Prion Protein (PrP) Formation in a Cell-Free System Using Baculovirus and Insect Cell-derived Recombinant PrP