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A key molecular event in prion diseases is the conversion of cellular prion protein (PrP c ) into an abnormal misfolded conformer (PrP sc ). The PrP c  N-terminal domain plays a central role in PrP c  functions and in prion propagation. Because mammalian PrP c  is found as a full-length and N-terminally truncated form, we examined the presence and amount of PrP c  C-terminal fragment in the brain of different species. We found important variations between primates and rodents. In addition, our data show that the PrP c  fragment is present in detergent-resistant raft domains, a membrane domain of critical importance for PrP c  functions and its conversion into PrP sc .

Truncated PrP c in mammalian brain: interspecies variation and location in membrane rafts