We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Mapping the antigenicity of copper-treated cellular prion protein with the scrapie isoform.
- Authors
Wong, B.-S.; Li, R.; Kang, S.-C.; Liu, T.; Pan, T.; Greenspan, N. S.; Wisniewski, T.; Brown, D. R.; Sy, M.-S.; Sassoon, J.
- Abstract
When recombinant and cellular prion protein (PrPC) binds copper, it acquires properties resembling the scrapie isoform (PrPSc), namely protease resistance, detergent insolubility and increased β sheet content. However, whether the conformations of PrPC induced by copper and PrPSc are similar has not been studied in great detail. Here, we use a panel of seven monoclonal antibodies to decipher the epitopes on full-length mouse PrPC that are affected by exogenous copper, and to compare the antigenicity of the copper-treated full-length PrPC with the full-length PrPSc present in scrapie-infected mouse brains. In the presence of copper, we found that epitopes along residues 115–130 and 153–165 become more accessible on PrPC. These regions correspond to the two β sheet strands in recombinant PrP and they were proposed to be important for prion conversion. However, when we compared the antibody-binding patterns between full-length PrPC with full-length PrPSc and between copper-treated full-length PrPC with full-length PrPSc, antibody binding to residues 143–155 and 175–185 was consistently increased on PrPSc. Collectively, our results suggest that copper-treated full-length PrPC does not resemble full-length PrPSc, despite acquiring PrPSc-like properties. In addition, since each full-length protein reacts distinctively to some of the antibodies, this binding pattern could discriminate between PrPC and PrPSc.
- Subjects
PRIONS; PROTEINS; COPPER; EPITOPES; SCRAPIE
- Publication
Cellular & Molecular Life Sciences, 2003, Vol 60, Issue 6, p1224
- ISSN
1420-682X
- Publication type
Article
- DOI
10.1007/s00018-003-3057-0