Strain-specific proteolytic processing of the prion protein in prion diseases of ruminants transmitted in ovine transgenic mice.
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 analysis. 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 transmissible spongiform encephalopathy infected mice essentially reflect the PrP proteolytic processing occurring in vivo.
Nicot
Simon
S
Agence Française de Sécurité Sanitaire des Aliments - Lyon, Unité ATNC, Lyon, France.
Baron
Thierry G M
TG
D000818:Animals; D001921:Brain / Q000378:metabolism; D002417:Cattle; D004195:Disease Models, Animal; D016643:Encephalopathy, Bovine Spongiform / Q000378:metabolism / Q000635:transmission*; D019286:Endopeptidase K / Q000378:metabolism; D051379:Mice; D008822:Mice, Transgenic; D018621:PrPC Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012608:Scrapie / Q000378:metabolism / Q000635:transmission*; D012756:Sheep; D013045:Species Specificity; D013820:Thermolysin / Q000378:metabolism
D018621:PrPC Proteins; D019286:Endopeptidase K; D013820:Thermolysin