Prion (PrPSc)-specific epitope defined by a monoclonal antibody

C. Korth (), B. Stierli, P. Streit, M. Moser, O. Schaller, R. Fischer, W. Schulz-Schaeffer, H. Kretzschmar, A. Raeber, U. Braun, F. Ehrensperger, S. Hornemann, R. Glockshuber, R. Riek, M. Billeter, K. Wüthrich and B. Oesch
Additional contact information
C. Korth: Prionics AG, University of Zürich
B. Stierli: Brain Research Institute, University of Zürich
P. Streit: Brain Research Institute, University of Zürich
M. Moser: Prionics AG, University of Zürich
O. Schaller: Prionics AG, University of Zürich
R. Fischer: Institut für Biochemie
W. Schulz-Schaeffer: Institut für Neuropathologie, Universitt Gttingen
H. Kretzschmar: Institut für Neuropathologie, Universitt Gttingen
A. Raeber: Institut für Neuropathologie, University of Zürich
U. Braun: Klinik für Wiederkuer-und Pferdemedizin, University of Zürich
F. Ehrensperger: Institut für Veterinrpathologie, University of Zürich
S. Hornemann: Institut für Molekularbiologie und Biophysik
R. Glockshuber: Institut für Molekularbiologie und Biophysik
R. Riek: Institut für Molekularbiologie und Biophysik
M. Billeter: Institut für Molekularbiologie und Biophysik
K. Wüthrich: Institut für Molekularbiologie und Biophysik
B. Oesch: Prionics AG, University of Zürich

Nature, 1997, vol. 390, issue 6655, 74-77

Abstract: Abstract Prions are infectious particles causing transmissible spongiform encephalopathies (TSEs). They consist, at least in part, of an isoform (PrPSc) of the ubiquitous cellular prion protein (PrPC). Conformational differences between PrPCand PrPScare evident from increased β-sheet content and protease resistance in PrPSc(refs 1,2,3). Here we describe a monoclonal antibody, 15B3, that can discriminate between the normal and disease-specific forms of PrP. Such an antibody has been long sought as it should be invaluable for characterizing the infectious particle as well as for diagnosis of TSEs such as bovine spongiform encephalopathy (BSE) or Creutzfeldt–Jakob disease (CJD) in humans. 15B3 specifically precipitates bovine, murine or human PrPSc, but not PrPC, suggesting that it recognizes an epitope common to prions from different species. Using immobilized synthetic peptides, we mapped three polypeptide segments in PrP as the 15B3 epitope. In the NMR structure of recombinant mouse PrP, segments 2 and 3 of the 15B3 epitope are near neighbours in space, and segment 1 is located in a different part of the molecule. We discuss models forthe PrPSc-specific epitope that ensure close spatial proximity of all three 15B3 segments, either by intermolecular contacts in oligomeric forms of the prion protein or by intramolecular rearrangement.

Date: 1997
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DOI: 10.1038/36337

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