NR AORE
AU Cashman,N.R.
TI An Epitope Selective for the Pathogenic Prion Protein
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Oral sessions OS-28
PT Konferenz-Vortrag
AB Conformational conversion of proteins in disease must be accompanied by molecular surface exposure of previously sequestered amino acid side chains. We find that low-pH induction of beta sheet structure in recombinant prion protein is associated with increased solvent accessibility of tyrosine. Antibodies directed against the prion protein repeat motif Tyr-Tyr-Arg recognize PrPsc, but not PrPc, by immunoprecipitation, plate capture immunoassay, and flow cytometry. Antibody binding to the pathological epitope is saturable, specific, and can be created in vitro by low pH treatment of normal brain prion. Conformation-selective exposure of the Tyr-Tyr-Arg epitope provides a probe for the distribution and structure of pathologically misfolded prion protein, and may lead to novel diagnostics and therapeutics for prion diseases.
AD Neil R. Cashman, University of Toronto, Canada
SP englisch
PO Deutschland