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Prion protein in sheep urine

Correspondence: ¹Corresponding Author: Olga Andrievskaia, Canadian Food Inspection Agency, Ottawa Laboratory Fallowfield, 3851 Fallowfield Road, Ottawa, Ontario K2H 8P9, Canada, e-mail: andrievskaiao{at}inspection.gc.ca

The misfolded form of cellular prion protein (PrP^C) is the main component of the infectious agent of transmissible spongiform encephalopathies and the validated biomarker for these diseases. The expression of PrP^C is highest in the central nervous system and has been found in peripheral tissues. Soluble PrP^C has been detected in cerebrospinal fluid, urine, serum, milk, and seminal plasma. In this study, attempts were made to characterize prion protein in urine samples from normal and scrapie-infected sheep. Urine samples from scrapie-infected sheep and age-matched healthy sheep were collected and analyzed by Western blot following concentration. A protease K–sensitive protein band with a molecular weight of approximately 27–30 kDa was visualized after immunoblotting with anti-PrP monoclonal antibodies to a C-terminal part of PrP^C, but not after immunoblotting with monoclonal antibodies to an N-terminal epitope of PrP^C or with secondary antibodies only. The amount of PrP^C in the urine of 49 animals (control group: n = 16; naturally scrapie-infected group: n = 33) was estimated by comparison with known amounts of ovine recombinant PrP in the immunoblot. Background concentration of PrP^C in urine was found to be 0–0.16 ng/ml (adjusted to the initial nonconcentrated volume of the urine samples). Seven out of 33 naturally scrapie-infected animals had an elevated level (0.3–4.7 ng/ml) of PrP^C in urine. The origin of PrP^C in urine and the reason for the increased level of PrP^C in scrapie-infected sheep urine has yet to be explored.

Key Words: Prion protein • scrapie • urine