Journal
BIOCHEMISTRY
Volume 45, Issue 47, Pages 14129-14139Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi061526k
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Funding
- NIAID NIH HHS [R21 AI058979, T32 AI007519] Funding Source: Medline
- NINDS NIH HHS [R01 NS046478] Funding Source: Medline
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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.
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