NR AURQ
AU Proft,J.; Kupfer,L.; Eiden,M.; Groschup,M.H.
TI Influence of the N-terminal region of prion protein on the formation of PrPres fragments in a cell-free conversion assay
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-14
PT Konferenz-Poster
AB
The central role in the pathogenesis of prion disease is the conversion of the normal cellular host prion protein PrPc into an abnormal pathogenic isoform PrPsc. This conversion process can be imitated in a cell-free conversion assay by adding purified PrPsc to recombinant PrPc, which is converted into a PK-resistant isoform PrPres.
This assay is used to investigate the influence of entire domains within the prion protein especially the N-terminus. Compared to the structured C-terminal core of PrPc the N-terminus of PrPc has the properties of a flexible random coil polypeptide. Here we used the cell-free conversion assay to study the biochemical influence of the flexible N-terminal tail of PrP on the formation of protease-resistant PrPres.
For this purpose several N-terminally deleted prion constructs were used during the conversion with different mouse passaged TSE strains. First data demonstrate an influence on fragment size and altered PK resistance of the newly formed PrPres fragments depending on the used TSE strain. Furthermore a capture ELISA will be established, to investigate the specific binding of the N-terminus to full-length prion protein as well as to deletion mutants.
AD Juliane Proft, Leila Kupfer, Martin Eiden, Martin H. Groschup, Institute for Novel and Emerging Infectious Diseases at the Friedrich-Loeffler-Institut, Isle of Riems
SP englisch
PO Deutschland
OR Tagungsband