J Gen Virol
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Journal of General Virology (2000), 81, 2555-2563.
© 2000 Society for General Microbiology

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Expression of unglycosylated mutated prion protein facilitates PrPSc formation in neuroblastoma cells infected with different prion strains

Carsten Korth1,2, Kiyotoshi Kanekob,1,2 and Stanley B. Prusiner1,2,3

Institute for Neurodegenerative Diseases1 and Departments of Neurology2 and Biochemistry and Biophysics3, Box 0518, University of California, San Francisco, CA 94143-0518, USA

Author for correspondence: Stanley Prusiner. Fax +1 415 476 8386.

Prion replication involves conversion of the normal, host-encoded prion protein PrPC, which is a sialoglycoprotein bound to the plasma membrane by a glycophosphatidylinositol anchor, into a pathogenic isoform, PrPSc. In earlier studies, tunicamycin prevented glycosylation of PrPC in scrapie-infected mouse neuroblastoma (ScN2a) cells but it was still expressed on the cell surface and converted into PrPSc; mutation of PrPC at glycosylation consensus sites (T182A, T198A) produced low steady-state levels of PrP that were insufficient to propagate prions in transgenic mice. By mutating asparagines to glutamines at the consensus sites, we obtained expression of unglycosylated, epitope-tagged MHM2PrP(N180Q,N196Q), which was converted into PrPSc in ScN2a cells. Cultures of uninfected neuroblastoma (N2a) cells transiently expressing mutated PrP were exposed to brain homogenates prepared from mice infected with the RML, Me7 or 301V prion strains. In each case, mutated PrP was converted into PrPSc as judged by Western blotting. These findings raise the possibility that the N2a cell line can support replication of different strains of prions.




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