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Updated: Aug 8, 2026
Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
Published on: March 10, 2015
Methods for the in vivo and in vitro analysis of [Het-s] prion infectivity
Laura Benkemoun1, Raimon Sabaté, Laurent Malato
1Laboratoire de Génétique Moléculaire des Champignons, IBGC UMR CNRS 5095, Université de Bordeaux 2, Bordeaux, France.
Abstract:
Prions have been described in mammals and fungi. The [Het-s] infectious genetic element of the filamentous fungus Podospora anserina is the prion form of the HET-s protein. This protein is involved in the control of a cell death reaction termed heterokaryon incompatibility. The infectious form of HET-s corresponds to a self-perpetuating amyloid. The purpose of the present paper is to describe the techniques that can be used to analyse [Het-s] prion propagation in vivo and HET-s amyloid aggregation in vitro. In addition, we report several methods that can be used to infect Podospora with recombinant HET-s amyloid.
Insights
This study details methods for analyzing the [Het-s] prion in Podospora anserina, focusing on its propagation in vivo and amyloid aggregation in vitro. Researchers also describe infecting fungi with recombinant HET-s amyloid.
Area of Science:
- Mycology
- Molecular Biology
- Prion Biology
Background:
- Prions, infectious proteins, are found in mammals and fungi.
- The [Het-s] element in Podospora anserina is a fungal prion.
- HET-s protein controls heterokaryon incompatibility, a cell death reaction.
Purpose of the Study:
- To present techniques for analyzing [Het-s] prion propagation in vivo.
- To describe methods for studying HET-s amyloid aggregation in vitro.
- To report on infecting Podospora with recombinant HET-s amyloid.
Main Methods:
- In vivo analysis of prion propagation.
- In vitro assessment of amyloid aggregation.
- Infection of Podospora with recombinant HET-s amyloid.
Main Results:
- Established techniques for in vivo [Het-s] prion propagation analysis.
- Developed methods for in vitro HET-s amyloid aggregation studies.
- Successfully infected Podospora fungi with recombinant HET-s amyloid.
Conclusions:
- The study provides a methodological framework for prion research in Podospora anserina.
- These techniques facilitate further investigation into fungal prion mechanisms.
- The findings contribute to understanding prion propagation and amyloid formation.
