NR AURO
AU Muyrers,J.; Lingappa,V.; Korth,C.
TI Monoclonal antibodies define conformational heterogeneity of the normal prion protein
QU TSE-Forum, 6. Kongress - Nationale TSE-Forschungsplattform, Greifswald 26.6.-28.6.2006, Poster: Struktur und molekulare Mechanismen MOL-12
PT Konferenz-Poster
AB
The physiological function of the normal cellular prion protein PrPc is still unknown. In vitro translation experiments suggested that the population of PrPc was conformationally heterogeneous but sensitive detection of these PrPc isoforms in vivo has been limited due to the absence of high affinity monoclonal antibodies.
Here we present antibody 19B10 that specifically recognizes a conformational epitope in an unglycosylated PrP species that overlaps with NTMPrP from in vitro translation studies. Serial immunoprecipitation experiments from brain homogenates or cell lysates indicate that seemingly "universal" mAB 6H4 does not deplete the 19B10 antigen from brain homogenates. Use of 19B10 in immunofluorescence staining of cells overexpressing wildtype, NTM or CTM isoforms of PrP demonstrate unique compartmental staining suggesting a unique biological role.
In conclusion, we present evidence for 1. conformational heterogeneity of PrPc and 2. mAB 19B10 defining a unique PrPc isoform of yet unknown function.
AD Janine Muyrers, Carsten Korth, University of Duesseldorf, Germany; Vishwanath Lingappa, University of California San Francisco, USA
SP englisch
PO Deutschland
OR Tagungsband