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Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
Published on: March 10, 2015
A simple, versatile and sensitive cell-based assay for prions from various species.
Zaira E Arellano-Anaya1, Jimmy Savistchenko, Jacinthe Mathey
1UMR Institut National de la Recherche Agronomique Ecole Nationale Vétérinaire de Toulouse 1225, Interactions Hôte Agent Pathogène, Toulouse, France.
Plos One
|June 10, 2011
Summary
A new RK13 cell line allows sensitive detection and quantification of diverse prion strains, including those from sheep and cervids. This method reduces cell culture work and may replace animal bioassays for prion research.
Area of Science:
- Veterinary Medicine
- Neuroscience
- Biochemistry
Background:
- Prion infectivity detection is vital for research and diagnostics.
- Current cell-based assays are limited to specific prion strains, necessitating animal bioassays.
- A broader range of prion detection methods is needed.
Purpose of the Study:
- To develop a robust and sensitive cell-based assay for quantifying diverse prion strains.
- To evaluate the RK13 cell line's permissiveness to various prion agents.
- To reduce the workload associated with prion titration.
Main Methods:
- Utilized the RK13 epithelial cell line for prion detection.
- Tested RK13 cells with mouse-adapted and natural prion strains from sheep and cervids.
- Developed a simplified RK13 cell assay procedure without subcultivation.
- Investigated prion binding to culture plastic.
Main Results:
- RK13 cells are permissive to mouse, bank vole, sheep, and cervid prion strains.
- The RK13 cell assay provides robust and sensitive detection of mouse and ovine prions.
- The assay procedure significantly reduces cell culture work by eliminating subcultivation.
- Prions bind to culture plastic and are quantitatively detected by the RK13 cells.
Conclusions:
- The RK13 cell line offers a versatile platform for quantifying a wide range of prions.
- This simplified cell assay can facilitate routine prion titration, potentially replacing animal bioassays.
- The findings will advance fundamental and applied prion research by enabling broader prion quantification.
