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Detection of the disease-associated isoform of the prion protein in formalin-fixed tissues by Western blot

Correspondence: ¹Corresponding Author: Eric M. Nicholson, Virus and Prion Diseases of Livestock Research Unit, National Animal Disease Center, USDA, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA 50010. eric.nicholson{at}ars.usda.gov

Clinical signs of prion disease are not specific and include a variety of differential diagnoses. Serological tests and nucleic acid–based detection methods are not applicable to prion-disease-agent detection because of the unusual nature of the infectious agent. Prion-disease diagnosis is primarily conducted by means of immunodetection of the infectious agent, typically by at least 2 distinct procedures with immunohistochemistry and Western blot being the most informative. These approaches differ in the need for formalin-fixed and frozen or fresh tissue respectively. This work describes a method for the detection of the disease-associated isoform of the prion protein by Western blot using formalin-fixed tissues. The approach requires only minimal modification of existing Western-blot procedures and could readily be incorporated into existing detection schemes for confirmatory purposes when fresh or frozen tissues are unavailable.

Key Words: Formalin • prion • prion protein (PrP) • scrapie • spongiform encephalopathy • transmissible spongiform encephalopathies (TSE) • Western blot

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				R. A. Kunkle, E. M. Nicholson, S. Lebepe-Mazur, D. L. Orcutt, M. L. Srinivas, J. J. Greenlee, D. P. Alt, and A. N. Hamir Western blot detection of PrPSc in archived paraffin-embedded brainstem from scrapie-affected sheep J Vet Diagn Invest, July 1, 2008; 20(4): 522 - 526. [Abstract] [Full Text] [PDF]