Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2006 Nov 28;45(47):14129-39.
doi: 10.1021/bi061526k.

The Stoichiometry of Host PrPC Glycoforms Modulates the Efficiency of PrPSc Formation in Vitro

Affiliations

The Stoichiometry of Host PrPC Glycoforms Modulates the Efficiency of PrPSc Formation in Vitro

Koren A Nishina et al. Biochemistry. .

Abstract

A central event in the formation of infectious prions is the conformational change of a host-encoded glycoprotein, PrPC, into a pathogenic isoform, PrPSc. However, the molecular requirements for efficient PrP conversion remain unknown. In this study, we employed the recently developed protein misfolding cyclic amplification (PMCA) and scrapie cell assay (SCA) techniques to study the role of N-linked glycosylation on prion formation in vitro. The results show that unglycosylated PrPC molecules are required to propagate mouse RML prions, whereas diglycosylated PrPC molecules are required to propagate hamster Sc237 prions. Furthermore, the formation of Sc237 prions is inhibited by substoichiometric levels of hamster unglycosylated PrPC molecules. Thus, interactions between different PrPC glycoforms appear to control the efficiency of prion formation in a species-specific manner.

Similar articles

See all similar articles

Cited by 48 articles

See all "Cited by" articles

Publication types

LinkOut - more resources

Feedback