Detection of PrPSc in peripheral tissues of clinically affected cattle after oral challenge with BSE
2012
Franz, Martin | Eiden, Martin | Balkema-Buschmann, Anne | Greenlee, J. | Schätzl, H. | Fast, Christine | Richt, J. | Hildebrandt, J.-P. | Groschup, Martin H.
Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative prion disease that mainly affects cattle. Transmission of BSE to humans caused a variant form of Creutzfeldt-Jakob disease (vCJD). Following infection the protease-resistant, disease-associated isoform of prion protein (PrPSc) accumulates in the central nervous system and in other tissues. Many countries have defined bovine tissues that may contain prions as specified risk materials (SRMs), which must not enter the human or animal food chains and therefore must be discarded. Ultrasensitive techniques such as the protein misfolding cyclic amplification (PMCA) have been developed to detect PrPSc when present in miniscule amounts that are not readily detected by other diagnostic methods such as immunohistochemistry or western blot. This study was conducted to determine when and where PrPSc can be found by PMCA in cattle orally challenged with BSE. A total of 48 different tissue samples from 4 orally BSE-infected cattle at clinical stages of disease were examined using a standardized PMCA protocol. The protocol used brain homogenate from bovine PrP transgenic mice (Tgbov XV) as substrate and three consecutive rounds of PMCA. Using this protocol PrPSc was found in brain, spinal cord, nerve ganglia, optic nerve, and Peyer's patches. We could confirm the presence of PrPSc in adrenal gland as well as in mesenteric lymph node - a finding, which was recently reported by another group. Interestingly, additional positive results were obtained for the first time in oesophagus, abomasum, rumen, and rectum of clinically affected cattle.
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