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Strain-specific proteolytic processing of the prion protein in prion diseases of ruminants transmitted in ovine transgenic mice

Agence Française de Sécurité Sanitaire des Aliments, Lyon, France

¹ E-mail: t.baron{at}lyon.afssa.fr

The cerebral prion protein (PrP) isolated in the absence of proteinase K digestion, from ruminants prion sources transmitted to ovine transgenic mice, was studied by Western blot. A C2 PrP fragment, showing strain-specific cleavages similar to those observed after proteinase K or thermolysin digestion, accumulated in the brain. "CH1641-like" scrapie was characterized by the unique accumulation of a more C-terminally cleaved PrP fragment (CTF14). A similar, protease-resistant, PrP product was observed after proteinase K or thermolysin digestion. Whereas classical BSE appeared highly resistant to thermolysin digestion, CH1641 and "CH1641-like" natural isolates did not show any remarkable feature regarding resistance to thermolysin. Thus the molecular strain-specific features in the brain of TSE-infected mice essentially reflect the PrP proteolytic processing occurring in vivo.

Received 18 June 2009; accepted 9 October 2009.