Abstract

An increasing number of scrapie cases with atypical characteristics, designated Nor98, have recently been recognised. The prominent fast migrating band in the distinct Nor98 western immunoblot electrophoretic profile of prion protein (PrP) after proteinase K (PK) treatment was determined to be 7 kDa and was accordingly designated Nor98-PrP7. The antigenic composition of Nor98-PrP7, as assayed by a panel of anti-PrP antibodies, revealed that this fragment comprised a midregion of PrP from around amino acid (aa) residue 85 to 150. PK-resistant N- and C-terminally truncated fragments spanning the midregion of PrP have previously only been observed in the genetic prion disorder Gerstmann-Sträussler-Scheinker disease. We show that the long-term PK-resistance of Nor98-PrP7 is reduced compared to that of PrPres in classical scrapie. A previously unidentified PK-resistant C-terminal PrP fragment of around 24 kDa was detected and its PK-resistance was investigated. Antigenic determination suggested a fragment approximately spanning aa residues 120 to 233. The existence of two PK-resistant PrP fragments that share an overlapping region suggest that at least two distinct PrP conformers with different PK-resistant cores are present in brain extracts from Nor98 affected sheep. The structural gene of PrP in three Nor98 affected sheep was analysed but no mutations were found that could be correlated to the aberrant PK-resistant profile observed

Published in

Conference

2nd Meeting of the Swedish Molecular Virology Network, Skytteholm, May 7-8, 2007

SLU Authors

• Wik, Lotta

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Linne, Tommy

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Animal and Dairy Science
Veterinary Science


Permanent link to this page (URI)

https://res.slu.se/id/publ/22693