Abstract

We have compared the posttranslational processing and the release of the wild-type and a deletion mutant of the bovine prion protein (boPrP) expressed in transfected cells, by western immunoblotting and radioactive pulse-chase labeling analyses. By creating a deletion spanning the c1 cleavage site in boPrP, the mode of release of boPrP from the cell can be affected, indicating the importance of this cleavage for the processing of the prion proteins. It is of large interest to investigate the underlying mechanisms for targeting prion protein to proteolytic, phospholipase-mediated or exosome-mediated release pathways, since it was recently reported (Fevrier et al., 2004) that PrPSc – containing exosomes released from prion-infected cells were infectious. The identification of infectious exosomes suggests exosome release as a mean of spreading prions between cells

Published in

Conference

2nd International Symposium on The new Prion Biology: Basic Science, Diagnosis and Therapy

SLU Authors

• Klingeborn, Mikael

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Wik, Lotta

  • Department of Molecular Biosciences, Swedish University of Agricultural Sciences
    

• Willander, Hanna

  • Department of Animal 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/23569