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Propagation of a protease-resistant form of prion protein in long-term cultured human glioblastoma cell line T98G

¹ Division of Microbiology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan
² Laboratory of Immunobiology, Graduate School of Biosphere Science, Hiroshima University, 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739-8528, Japan
³ Division of Food Additives, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan
⁴ Division of Biochemistry and Immunochemistry, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan

Correspondence
Yutaka Kikuchi
kikuchi{at}nihs.go.jp

Human prion diseases, such as Creutzfeldt–Jakob disease (CJD), a lethal, neurodegenerative condition, occur in sporadic, genetic and transmitted forms. CJD is associated with the conversion of normal cellular prion protein (PrP^C) into a protease-resistant isoform (PrP^res). The mechanism of the conversion has not been studied in human cell cultures, due to the lack of a model system. In this study, such a system has been developed by culturing cell lines. Human glioblastoma cell line T98G had no coding-region mutations of the prion protein gene, which was of the 129 M/V genotype, and expressed endogenous PrP^C constitutively. T98G cells produced a form of proteinase K (PK)-resistant prion protein fragment following long-term culture and high passage number; its deglycosylated form was approximately 18 kDa. The PK-treated PrP^res was detected by immunoblotting with the mAb 6H4, which recognizes residues 144–152, and a polyclonal anti-C-terminal antibody, but not by the mAb 3F4, which recognizes residues 109–112, or the anti-N-terminal mAb HUC2-13. These results suggest that PrP^C was converted into a proteinase-resistant form of PrP^res in T98G cells.