@article{mbs:/content/journal/jgv/10.1099/0022-1317-81-10-2565, author = "Iniguez, Volga and McKenzie, Debbie and Mirwald, Jean and Aiken, Judd", title = "Strain-specific propagation of PrPSc properties into baculovirus-expressed hamster PrPC", journal= "Journal of General Virology", year = "2000", volume = "81", number = "10", pages = "2565-2571", doi = "https://doi.org/10.1099/0022-1317-81-10-2565", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-81-10-2565", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The conversion of the cellular isoform of the prion protein (PrPC) to the abnormal disease-associated isoform (PrPSc) has been simulated in cell-free conversion reactions in which PrPSc-enriched preparations induce the conformational transition of PrPC into protease-resistant PrP (PrP-res). We explored the utility of recombinant hamster (Ha)PrPC purified from baculovirus-infected insect cells (bacHaPrPC) as a replacement for mammalian-derived HaPrPC in the conversion reactions. Protease-resistant recombinant HaPrP was generated after incubation of 35S-bacHaPrPC with PrPSc-enriched preparations. Moreover strain-specific PrP-res was also reproduced using insect-cell derived HaPrPC and PrPSc from two different strains of hamster-adapted transmissible mink encephalopathy, designated hyper (HY) and drowsy (DY). Two strain-mediated properties were tested: (i) molecular mass of the protease-digested products and (ii) relative resistance to proteinase K (PK) digestion. Similar to in vivo generation of PrPHY and PrPDY, the converted products selectively reproduced both characteristics, with the DY conversion product being smaller in size and less resistant to PK digestion than the HY product. These data demonstrate that non-mammalian sources of recombinant HaPrP can be converted into PK-resistant form and that strain-mediated properties can be transmitted into the newly formed PrP-res.", }