%0 Journal Article %A Kikuchi, Yutaka %A Kakeya, Tomoshi %A Sakai, Ayako %A Takatori, Kosuke %A Nakamura, Naoto %A Matsuda, Haruo %A Yamazaki, Takeshi %A Tanamoto, Ken-ichi %A Sawada, Jun-ichi %T Propagation of a protease-resistant form of prion protein in long-term cultured human glioblastoma cell line T98G %D 2004 %J Journal of General Virology, %V 85 %N 11 %P 3449-3457 %@ 1465-2099 %R https://doi.org/10.1099/vir.0.80043-0 %I Microbiology Society, %X 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 (PrPC) into a protease-resistant isoform (PrPres). 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 PrPC 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 PrPres 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 PrPC was converted into a proteinase-resistant form of PrPres in T98G cells. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80043-0