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Prion diseases are fatal neurodegenerative diseases which occur as sporadic, genetic, and transmissible disorders. A molecular hallmark of prion diseases is the conformational conversion of the host-encoded cellular form of the prion protein (PrP C ) into its misfolded pathogenic isoform (PrP Sc ). PrP Sc  is the main component of the pathological and infectious prion agent. The study of the conversion mechanism from PrP C  to PrP Sc  is a major field in prion research. PrP C  is glycosylated and attached to the plasma membrane via its glycosyl phosphatidyl inositol (GPI)-anchor. In this study we established and characterised the expression of fully posttranslationally modified mammalian Syrian golden hamster PrP C  in the yeast  Pichia pastoris  using native PrP C -specific N- and C-terminal signal sequences.  In vivo  as well as  in vitro -studies demonstrated that the signal sequences controlled posttranslational processing and trafficking of native PrP C , resulting in PrP C  localised in the plasma membrane of  P. pastoris . In addition, the glycosylation pattern of native PrP C  could be confirmed.

Expression and characterisation of fully posttranslationally modified cellular prion protein in Pichia pastoris