Evaluation of Infective Property of Recombinant Prion Protein Amyloids in Cultured Cells Overexpressing Cellular Prion Protein.
10.3346/jkms.2014.29.12.1604
- Author:
Dae Hwan KIM
1
;
Hye Mi LEE
;
Chongsuk RYOU
Author Information
1. Department of Pharmacy, College of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University, Ansan, Korea. cryou2@hanyang.ac.kr
- Publication Type:Original Article
- Keywords:
Prions;
Recombinant Prion Protein;
Aggregates;
Amyloid;
Infectivity
- MeSH:
Animals;
Cell Line;
Kidney/*metabolism/*pathology;
Mice;
PrPSc Proteins/*metabolism;
Prion Diseases/*metabolism/*pathology;
Prions/*metabolism;
Rabbits;
Recombinant Proteins/*metabolism;
Up-Regulation
- From:Journal of Korean Medical Science
2014;29(12):1604-1609
- CountryRepublic of Korea
- Language:English
-
Abstract:
Misfolded isoform of prion protein (PrP), termed scrapie PrP (PrP(Sc)), tends to aggregate into various fibril forms. Previously, we reported various conditions that affect aggregation of recombinant PrP into amyloids. Because amyloidogenesis of PrP is closely associated with transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease in humans, we investigated infectivity of recombinant PrP amyloids generated in vitro. Using cultured cell lines which overexpress cellular PrP of different species, we measured the level of de novo synthesized PrP(Sc) in cells inoculated with recombinant mouse PrP amyloids. While PrP-overexpressing cells were susceptible to mouse-adapted scrapie prions used as the positive control, demonstrating the species barrier effect, infection with amyloids made of truncated recombinant PrP (PrP[89-230]) failed to form and propagate PrP(Sc) even in the cells that express mouse cellular PrP. This suggests that infectivity of PrP amyloids generated in vitro is different from that of natural prions. Recombinant PrP (89-230) amyloids tested in the current study retain no or a minute level, if any, of prion infectivity.
