An Antibody to the aggregated synthetic prion protein peptide (PrP106-126) selectively recognizes disease-associated prion protein (PrPSc) from human brain specimens

M. Jones; D. Wight; V. McLoughlin; K. Norrby; J.W. Ironside; J.G. Connolly; C.F. Farquhar; I.R. MacGregor; M.W. Head

doi:10.1111/j.1750-3639.2008.00181.x

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An Antibody to the aggregated synthetic prion protein peptide (PrP106-126) selectively recognizes disease-associated prion protein (PrPSc) from human brain specimens

Journal article

Peer reviewed

An Antibody to the aggregated synthetic prion protein peptide (PrP106-126) selectively recognizes disease-associated prion protein (PrPSc) from human brain specimens

M. Jones, D. Wight, V. McLoughlin, K. Norrby, J.W. Ironside, J.G. Connolly, C.F. Farquhar, I.R. MacGregor and M.W. Head

Brain Pathology, Vol.19(2), pp.293-302

2009

DOI: https://doi.org/10.1111/j.1750-3639.2008.00181.x

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Abstract

Human prion diseases are characterized by the conversion of the normal host cellular prion protein (PrPC) into an abnormal misfolded form [disease‐associated prion protein (PrPSc)]. Antibodies that are capable of distinguishing between PrPC and PrPSc may prove to be useful, not only for the diagnosis of these diseases, but also for a better understanding of the molecular mechanisms involved in disease pathogenesis. In an attempt to produce such antibodies, we immunized mice with an aggregated peptide spanning amino acid residues 106 to 126 of human PrP (PrP106–126). We were able to isolate and single cell clone a hybridoma cell line (P1:1) which secreted an IgM isotype antibody [monoclonal antibody (mAb P1:1)] that recognized the aggregated, but not the monomeric form of the immunogen. When used in immunoprecipitation assays, the antibody did not recognize normal PrPC from non‐prion disease brain specimens, but did selectively immunoprecipitate full‐length PrPSc from cases of variant and sporadic Creutzfeldt–Jakob disease and Gerstmann–Straussler–Scheinker disease. These results suggest that P1:1 recognizes an epitope formed during the structural rearrangement or aggregation of the PrP that is common to the major PrPSc types found in the most common forms of human prion disease.

Details

Title: An Antibody to the aggregated synthetic prion protein peptide (PrP106-126) selectively recognizes disease-associated prion protein (PrPSc) from human brain specimens
Authors/Creators: M. Jones (Author/Creator) - Western General Hospital
D. Wight (Author/Creator) - Western General Hospital
V. McLoughlin (Author/Creator) - Strathclyde Institute of Pharmacy and Biomedical Sciences
K. Norrby (Author/Creator) - Western General Hospital
J.W. Ironside (Author/Creator) - Western General Hospital
J.G. Connolly (Author/Creator) - Strathclyde Institute of Pharmacy and Biomedical Sciences
C.F. Farquhar (Author/Creator) - Roslin Institute
I.R. MacGregor (Author/Creator) - SNBTS Products and Components R & D, National Science Laboratory, Edinburgh, UK.
M.W. Head (Author/Creator) - Western General Hospital
Publication Details: Brain Pathology, Vol.19(2), pp.293-302
Publisher: Wiley
Identifiers: 991005541191907891
Copyright: © 2008 The Authors; Journal Compilation © 2008 International Society of Neuropathology
Murdoch Affiliation: Murdoch University
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration
Citation topics: 1 Clinical & Life Sciences; 1.52 Neurodegenerative Diseases; 1.52.992 Prion Pathogenesis
Web Of Science research areas: Clinical Neurology; Neurosciences; Pathology
ESI research areas: Neuroscience & Behavior