PMID: 9445012Jan 28, 1998Paper

Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation

Journal of Virology
C HölscherAlexander Bürkle

Abstract

One hallmark of prion diseases is the accumulation of the abnormal isoform PrP(Sc) of a normal cellular glycoprotein, PrPc, which is characterized by a high content of beta-sheet structures and by its partial resistance to proteinase K. It was hypothesized that the PrP region comprising amino acid residues 109 to 122 [PrP(109-122)], which spontaneously forms amyloid when it is synthesized as a peptide but which does not display significant secondary structure in the context of the full-length PrPc molecule, should play a role in promoting the conversion into PrP(Sc). By using persistently scrapie-infected mouse neuroblastoma (Sc+-MNB) cells as a model system for prion replication, we set out to design dominant-negative mutants of PrPc that are capable of blocking the conversion of endogenous, wild-type PrPc into PrP(Sc). We constructed a deletion mutant (PrPc delta114-121) lacking eight codons that span most of the highly amyloidogenic part, AGAAAAGA, of PrP(109-122). Transient transfections of mammalian expression vectors encoding either wild-type PrPc or PrPc delta114-121 into uninfected mouse neuroblastoma cells (Neuro2a) led to overexpression of the respective PrPc versions, which proved to be correctly localized on the ext...Continue Reading

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