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Prion. 2014 Mar-Apr;8(2). pii: 28669. Epub 2014 Apr 10.

Comparison of 2 synthetically generated recombinant prions.

Author information

1
Key Laboratory of Brain Functional Genomics; Ministry of Education; Shanghai Key Laboratory of Brain Functional Genomics; School of Life Sciences; East China Normal University; Shanghai, PR China; Department of Molecular and Cellular Biochemistry; Ohio State University; Columbus, OH USA.
2
Department of Molecular and Cellular Biochemistry; Ohio State University; Columbus, OH USA.
3
Key Laboratory of Brain Functional Genomics; Ministry of Education; Shanghai Key Laboratory of Brain Functional Genomics; School of Life Sciences; East China Normal University; Shanghai, PR China.

Abstract

Prion is a protein-conformation-based infectious agent causing fatal neurodegenerative diseases in humans and animals. Our previous studies revealed that in the presence of cofactors, infectious prions can be synthetically generated in vitro with bacterially expressed recombinant prion protein (PrP). Once initiated, the recombinant prion is able to propagate indefinitely via serial protein misfolding cyclic amplification (sPMCA). In this study, we compared 2 separately initiated recombinant prions. Our results showed that these 2 recombinant prions had distinct biochemical properties and caused different patterns of spongiosis and PrP deposition in inoculated mice. Our findings indicate that various recombinant prions can be initiated in vitro and potential reasons for this variability are discussed.

KEYWORDS:

GuHCl denaturation assay; bioassay; histopathology; prion; recombinant PrP; recombinant prion; sPMCA

PMID:
24721728
PMCID:
PMC4189893
[Indexed for MEDLINE]
Free PMC Article

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