NR AURG
AU Eiden,M.; Groschup,M.H.
TI Synergistic and strain specific effects of BSE and scrapie prions in the cell-free conversion of recombinant prion protein
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-04
PT Konferenz-Poster
AB Transmissible spongiform encephalopathies (TSEs) are characterized by a structural change of the cellular PrPc into an abnormal form which is designated PrPsc or PrPres.,which is called conversion. Here we describe the conversion of murine PrPc by PrPsc by a modified nonradioactive cell-free conversion assay using bacterial prion protein that is converted into a proteinase K (PK) resistant fragment PrPres. According to this assay newly formed PrPres can be detected by an antibody that discriminates between the de novo PrPres and the PrPsc seed. PrPres formation is occurring in three phases: In the first 48 hours (h) a delay of PrPres formation (phase 1), followed by an increase to an maximum after approximately 72 h ( phase 2). Between 72h and 168 h no further increase was observed (phase 3). The conversion of prokaryotic PrPc by Me7 and BSE prions led to PrPres fragments which differed by about 1 kDa. Moreover, the coincubation of Me7 and BSE prions resulted in equal amounts of both Me7 and BSE derived PrPres fragments, but also to a significantly increased total amount of de novo generated PrPres. This result denotes a synergistic effect of both strains during cell-free conversion. It is yet unknown, whether such a cooperative action of BSE and scrapie prions also occurs in-vivo.
AD M.Eiden, M.H.Groschup, Institute for Novel and Emerging Infectious Diseases at the Friedrich-Loeffler-Institut, Isle of Riems
SP englisch
PO Deutschland
OR Tagungsband