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Updated: Aug 24, 2026
Detection of Abnormal Prion Protein by Immunohistochemistry
Published on: May 5, 2023
Detection of prion after decontamination procedures: comparative study of standard Western blot, filter retention and
J Solassol1, M Arlotto, S Lehmann
1Institut de Génétique Humaine, UPR 1142 du CNRS, 141 rue de la Cardonille, 34396 Montpellier Cedex 05, France.
Abstract:
Prion diseases such as Creutzfeldt-Jakob disease represent a unique infection control problem because the infectious agent exhibits an unusual resistance to conventional chemical and physical decontamination methods. We investigated the reliability and sensitivity of a filter retention assay and standard Western blot to detect the scrapie form of cellular prion protein (PrPSc), the most commonly used surrogate prion disease marker, on tissue infected samples, treated with five commercially available decontamination solutions currently used in hospitals. Major discrepancies were observed between the two immunoblot methods. By using Western blot, we observed that three decontamination solutions have a strong ability to reduce PrPSc levels, whereas in the filter assay, none have this effect and two even enhanced the detection of PrPSc. We used an original and rapid ex vivo approach called the scrapie-cell assay to analyse the persistence of infectivity on scrapie-treated tissues. We observed that tissues remained infectious after treatment with the decontaminant in concordance with in vivo data. This study suggests that conventional PrPSc detection methods are not adapted for the rapid study of a large number of prion decontaminants tested on infectious tissues, and that the scrapie-cell assay could be proposed as a relevant alternative method.
Insights
Detecting prion diseases like Creutzfeldt-Jakob disease is challenging due to agent resistance. Conventional methods for detecting prion protein (PrPSc) showed discrepancies, suggesting a need for better assays like the scrapie-cell assay.
Area of Science:
- Infectious diseases
- Biochemistry
- Microbiology
Background:
- Prion diseases pose unique infection control challenges due to the agent's resistance to decontamination.
- The scrapie form of cellular prion protein (PrPSc) is a key marker for prion diseases.
Purpose of the Study:
- To evaluate the reliability and sensitivity of Western blot and filter retention assays for detecting PrPSc.
- To assess the effectiveness of hospital-used decontamination solutions on prion-infected tissues.
- To introduce and validate the scrapie-cell assay as an alternative method for prion infectivity analysis.
Main Methods:
- Tissue samples infected with scrapie were treated with five commercial decontamination solutions.
- PrPSc detection was performed using standard Western blot and a filter retention assay.
- Prion infectivity was analyzed using an ex vivo scrapie-cell assay.
Main Results:
- Significant discrepancies were observed between Western blot and filter assay results for PrPSc detection.
- Western blot indicated three solutions reduced PrPSc levels, while the filter assay showed no reduction, with two solutions enhancing detection.
- The scrapie-cell assay confirmed that tissues remained infectious after decontamination, aligning with in vivo data.
Conclusions:
- Conventional PrPSc detection methods (Western blot, filter assay) are not suitable for rapidly evaluating prion decontaminants on infectious tissues.
- The scrapie-cell assay demonstrates potential as a relevant and sensitive alternative for assessing prion infectivity after decontamination treatments.
