These two authors contributed equally to the work.
Distinct immunohistochemical localization in Kuru plaques using novel anti-prion protein antibodies
Article first published online: 19 MAR 2008
2008 The Societies and Blackwell Publishing Asia Pty Ltd
Microbiology and Immunology
Volume 52, Issue 1, pages 25–29, January 2008
How to Cite
Hosokawa, T., Ono, F., Tsuchiya, K., Sato, I., Takeyama, N., Ueda, S., Zanusso, G., Takahashi, H., Sata, T., Sakudo, A., Suguira, K., Baj, A., Toniolo, A., Yoshikawa, Y. and Onodera, T. (2008), Distinct immunohistochemical localization in Kuru plaques using novel anti-prion protein antibodies. Microbiology and Immunology, 52: 25–29. doi: 10.1111/j.1348-0421.2008.00007.x
- Issue published online: 19 MAR 2008
- Article first published online: 19 MAR 2008
- Received 23 May 2007; accepted: 17 October 2007.
- bovine spongiform encephalopathy;
- Creutzfeldt-Jakob disease;
By immunizing Prnp-knockout mice with synthetic polypeptides, a panel of mAbs directed to bovine PrPC was obtained. The mAb panel was characterized by the ELISA method, where synthetic polypeptides were used for epitope mapping. Different reactivity patterns were identified. The ability of these mAbs to detect abnormal PrPSc in CJD cases was studied by immunohistochemistry. All mAbs were tested for PrPSc in murine, bovine, monkey and human brain tissues. Three mAbs recognized the fragmented PrP epitope in our ELISA. Antibody 1D12 was strongly reactive to ovine and squirrel monkey tissues infected with a scrapie agent, although non-reactive to scrapie-infected mouse tissues. Antibody 2D8 was clearly reactive to type-2 but not type-1 CJD human tissues. Of particular interest was the reactivity of mAb 6C4 with the inner structure of Kuru plaques (peripheral pattern) in a type-2 CJD case and mAb T2, 1D12, 2B11, 2D8, 4B5 and 6G3-2 with the central area (central pattern). The fact that different anti-PrP mAbs possess distinct staining properties suggests that the PrPc to PrPSc conversion might involve a multiple-step process.