NR ATKG
AU Maddison,B.C.; Conlon,H.E.; Gough,K.C.; Owen,J.P.; James,R.F.; Kilpatrick,J.B.; Jackman,R.; Whitelam,G.C.
TI The development of antibodies specific for conformational isomers of ovine PrP
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Diagnosis DIA-18
PT Konferenz-Poster
AB
Currently, all approved TSE diagnostics are immunoassays that detect PrPsc in post mortem samples. The limitation of such tests is primarily one of analytical sensitivity inherent in the need for sample pre-treatment to eliminate the normal cellular form of the prion protein (PrPc). These procedures significantly reduce the levels of PrPsc in the extract applied to the endpoint immunoassay. The development of immunoreagents capable of binding specifically to PrPsc in the presence of PrPc is an important step in overcoming these constraints.
Various lines of evidence suggest that a beta sheet-rich isomer of recombinant PrP may be structurally similar to PrPsc and consequently these two proteins may share common epitopes. Here, we have produced a novel form of recombinant ovine PrP which maintains a stable, soluble beta sheet-rich conformation at pH 8.0. This beta-sheet rich conformation has been used as an immunogen in transgenic Prnp0/0 mice for the selection of monoclonal antibodies. Resultant antibodies were evaluated in immunoassays and a beta-form-specific antibody selected. The binding specificities to brain PrP isoforms are discussed.
AD B.Maddison, K.C.Gough, J.P.Owen, J.B.Kilpatrick, ADAS UK Ltd., UK; H.E.Conlon, R.F.James, G.C.Whitelam, University of Leicester, UK; R.Jackman, Veterinary Laboratory Agency, UK
SP englisch
PO Deutschland