Abstract
BackgroundThe bovine spongiform encephalopathy (BSE) epidemic and the emergence of a new human variant of Creutzfeldt-Jakob Disease (vCJD) have led to profound changes in the production and trade of agricultural goods. The rapid tests currently approved for BSE monitoring in slaughtered cattle are all based on the detection of the disease related isoform of the prion protein, PrPd, in brain tissue and consequently are only suitable for post-mortem diagnosis. Objectives: In instances such as assessing the health of breeding stock for export purposes where post-mortem testing is not an option, there is a demand for an ante-mortem test based on a matrix or body fluid that would permit easy access and repeated sampling. Urine and urine based analyses would meet these requirements.ResultsTwo dimensional differential gel eletrophoresis (2D-DIGE) and mass spectrometry analyses were used to identify proteins exhibiting differential abundance in the urine of BSE infected cattle and age matched controls over the course of the disease. Multivariate analyses of protein expression data identified a single protein able to discriminate, with 100% accuracy, control from infected samples. In addition, a subset of proteins were able to predict with 85% ± 13.2 accuracy the time post infection that the samples were collected.ConclusionThese results suggest that in principle it is possible to identify biomarkers in urine useful in the diagnosis, prognosis and monitoring of disease progression of transmissible spongiform encephalopathy diseases (TSEs).
Highlights
The bovine spongiform encephalopathy (BSE) epidemic and the emergence of a new human variant of Creutzfeldt-Jakob Disease have led to profound changes in the production and trade of agricultural goods
The rapid tests currently approved for BSE monitoring in slaughtered cattle are all based on the detection of the disease related isoform of the prion protein, PrPd, in brain tissue and are only suitable for post-mortem diagnosis
The results indicate that biomarkers in urine may be useful in the diagnosis, prognosis and monitoring of disease progression of transmissible spongiform encephalopathy diseases (TSEs)
Summary
The bovine spongiform encephalopathy (BSE) epidemic and the emergence of a new human variant of Creutzfeldt-Jakob Disease (vCJD) have led to profound changes in the production and trade of agricultural goods. The rapid tests currently approved for BSE monitoring in slaughtered cattle are all based on the detection of the disease related isoform of the prion protein, PrPd, in brain tissue and are only suitable for post-mortem diagnosis. Bovine Spongiform Encephalopathy (BSE) was first described in the UK in 1985 and became an epidemic that peaked with 37, 280 cases reported in 1992[1]. A post-mortem examination revealing characteristic deposits of an insoluble host encoded protein, astrocytosis and spongiosis is required for definitive diagnosis. The characteristic protein deposits are formed by the accumulation of misfolded isoforms of a host-encoded protein, PrPc, or prion protein. The term PrPd is used to denote the presence of abnormal accumulations or isoforms of PrP detected by any method without prejudice as to its biochemical properties, its infectivity, source or host range[3]
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