NR AWHQ
AU Jones,M.; McLoughlin,V.; Norrby,K.; Conolly,J.G.; Farquhar,C.F.; MacGregor,I.R.; Head,M.W.
TI A novel monoclonal antibody that selectively recognises abnormal prion protein
QU International Conference - Prion 2006: Strategies, advances and trends towards protection of society - 3.10.-6.10.2006, Torino, Italy, Lingotto Conference Centre - Oral sessions ORAL-46
PT Konferenz-Vortrag
AB The aggregated prion protein peptide (PrP106-126) has been used extensively as a model of prion disease neurotoxicity. We reasoned that the aggregation process may generate epitopes that are not present on the monomeric peptide, and that such epitopes may be shared with the PrPsc that accumulates in human and animal prion diseases. In an attempt to generate monoclonal antibodies that recognise such putative PrPsc-specific epitopes, we immunised PrP null mice with the aggregated PrP106-126peptide. We then screened resultant monoclonal antibodies with monomeric and aggregated forms of PrP106-126 and identified an antibody (designated P1.1) that binds to the aggregated, but not the monomeric PrP106-126 peptide. Next we determined the reactivity of P1.1 for abnormal full-length mouse and human prion protein. P1.1 selectively recognises aggregated, in preference tomonomeric, recombinant mouse PrP and selectively immunoprecipitates PrPsc from CJD brain homogenates. These data indicate that P1.1 is a PrPsc-selective reagent and imply that structural aspects of the aggregated PrP106-126 peptide are also features of the abnormal disease-associated PrP found in vivo. This work was supported by the UK Department of Health.
AD M. Jones, K. Norrby, M.W. Head: National CJD Surveillance Unit, School of Molecular & Clinical Medicine, University of Edinburgh, Edinburgh, UK; V. McLoughlin, J.G. Connolly: Department of Physiology and Pharmacology, University of Strathclyde, Glasgow, UK; C.F. Farquhar: Neuropathogenesis Unit, Institute for Animal Health, Edinburgh, UK; I.R. MacGregor: SNBTS Products and Components R & D, National Science Laboratory, Edinburgh, UK. E-mail: m.w.head@ed.ac.uk
SP englisch
PO Italien