Comparison of French natural scrapie isolates with bovine spongiform encephalopathy and experimental scrapie infected sheep.
We compared the glycoform pattern of the abnormal prion protein (PrP(Sc)) detected by immunoblotting in 21 sheep with natural scrapie, from 21 different outbreaks identified in France since 1996, with a bovine spongiform encephalopathy (BSE)-infected sheep. All the natural scrapie isolates had a higher molecular mass of the unglycosylated PrP(Sc) than in BSE-infected sheep. In the latter case, this molecular mass appeared identical to that found in the CH 1641 experimental scrapie strain (type C pattern), whereas in natural scrapie cases it was similar to that found in the SSBP/1 experimental scrapie strains. These results suggest that all French natural scrapie isolates studied so far would belong, as SSBP/1, to the group of scrapie cases with type A electrophoretic pattern.
Baron
T G
TG
Agence Française de Sécurité Sanitaire des Aliments, 69364, Lyon, France. t.baron@lyon.afssa.fr
Madec
J Y
JY
Calavas
D
D
Richard
Y
Y
Barillet
F
F
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D016643:Encephalopathy, Bovine Spongiform / Q000378:metabolism*; D005602:France / Q000453:epidemiology; D006031:Glycosylation; D008970:Molecular Weight; D018620:PrPSc Proteins / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D012608:Scrapie / Q000453:epidemiology / Q000378:metabolism*; D012756:Sheep
D018620:PrPSc Proteins