Abstract
An abnormal isoform of prion protein (PrP Sc), which is composed of the same amino acids as cellular PrP (PrP C) and has proteinase K (PK)-resistance, hypothetically converts PrP C into PrP Sc. To investigate the region important for PrP Sc production, we examined the levels of PrP Sc in PrP gene-deficient cells (HpL3-4) expressing PrP C deleted of various regions including the octapeptide repeat region (OR) or hydrophobic region (HR). After Chandler or Obihiro prion infection, PrP Sc was produced in HpL3-4 cells expressing wild-type PrP C or PrP C deleted of HR at an early stage and further reduced to below the detectable level, whereas cells expressing PrP C deleted of OR showed no PrP Sc production. The results suggest that OR of PrP C is required for the early step of efficient PrP Sc production.
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