NR ALQF
AU Thackray,A.M.; Madec,J.Y.; Wong,E.; Morgan-Warren,R.; Brown,D.R.; Baron,T.G.M.; Bujdoso,R.
TI Detection of BSE, ovine scrapie PrPsc and normal PrPc by monoclonal antibodies raised to copper-refolded prion protein
QU Biochemical Journal 2002 Nov 12; Pt
PT journal article
AB PrP is a glycosylphosphatidylinositol (GPI)-linked cell-surface protein expressed by a wide variety of cells including those of the nervous system and the immune system. Several functions of PrPc have been proposed that may be associated with the capacity of this protein to bind copper. Here, we describe the generation of a panel of monoclonal antibodies raised to copper-refolded PrP, which may be used to analyse the normal and disease-associated forms of this protein. The anti-PrP monoclonal antibodies were reactive by Western blot and ELISA with recombinant murine PrPc refolded in the presence and absence of either copper or manganese, and with the VRQ and ARR allelic forms of recombinant ovine PrP c. FACS analysis of lymphoid cells using these monoclonal antibodies showed that wild type non-activated mouse lymphocytes expressed little if any PrP c. These monoclonal antibodies were shown to react with the unglycosylated and monoglycosylated forms of PrPsc in prion infected tissue samples from all the different species tested by Western blot. In addition, this analysis allowed the distinction between bovine spongiform encephalopathy (BSE) and scrapie PrPsc isolates from experimentally infected sheep on the basis of their different electrophoretic mobilities.
SP englisch