AI Article Synopsis
- The research aims to assess whether existing methods for extracting prion proteins (PrP) from formalin-fixed paraffin-embedded tissue (FFPET) can be used with a sensitive detection technique called real-time quaking induced conversion (RT-QuIC) for transmissible spongiform encephalopathies (TSEs).
- The study found that results from RT-QuIC using aqueous extracts of FFPET samples perfectly matched the TSE status of the samples.
- This method provides a way to diagnose TSEs in FFPET without needing organic solvents, thus minimizing chemical waste generated during the process.
Article Abstract
Objective: The goal of the research presented here is to determine if methods previously developed for the aqueous extraction of PrP from formalin-fixed paraffin-embedded tissue (FFPET) are applicable to the detection PrP by real-time quaking induced conversion (RT-QuIC). Previous work has utilized aqueous extraction of FFPET for detection of transmissible spongiform encephalopathies (TSEs) utilizing western blot and ELISA. This research extends the range of suitable methods for detection of TSEs in FFPET to RT-QuIC, which is arguably the most sensitive method to detect TSEs.
Results: We found complete agreement between the TSE status and the results from RT-QuIC seeded with the aqueous extract of FFPET samples. The method affords the diagnostic assessment TSE status by RT-QuIC of FFPET without the use of organic solvents that would otherwise create a mixed chemical-biological waste for disposal.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11403835 | PMC |
| http://dx.doi.org/10.1186/s13104-024-06886-6 | DOI Listing |
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