Location: Virus and Prion ResearchTitle: Enrichment of PrPSc in Formalin Fixed Paraffin Embedded Tissues Prior to Analysis by Western Blot) Author
Submitted to: Journal of Veterinary Diagnostic Investigation
Publication Type: Peer reviewed journal
Publication Acceptance Date: 1/27/2011
Publication Date: 7/1/2011
Citation: Nicholson, E.M. 2011. Enrichment of PrPSc in formalin-fixed, paraffin-embedded tissues prior to analysis by Western blot. Journal of Veterinary Diagnostic Investigation. 23(4):790-792. Interpretive Summary: This work reports an advance to a method to detect the prion protein, the causitve agent of transmissible spongiform encephalopathies (TSEs) such as bovine spongiform encephalopathy (BSE), scrapie, and chronic wasting disease (CWD). With this advance, the sensitivity of the detection is up to 5 times more sensitive than the previously published method, greatly enhancing the ability to use formalin-fixed paraffin embedded tissues for Western blot detection of TSEs.
Technical Abstract: Diagnosis of prion disease is primarily through immunodetection of the infectious agent. Typically, 2 distinct procedures are recommended for a definitive diagnosis with immunohistochemistry and Western blot providing the most information as to the specific isolate in question. In the past these approaches required formalin-fixed paraffin embedded tissue and fresh/frozen tissue respectively. This work describes an advance in methodology for Western blot analysis of formalin-fixed paraffin embedded tissues for the detection of PrP**Sc. With this modified procedure, 5 times the previously reported sample size may be used for analysis greatly enhancing the sensitivity of this procedure.