NR AXVU

AU Salta,E.; Panagiotidis,C.; Petrakis,S.; Eleftheriadis,E.; Arapoglou,F.; Karagiannis,D.; Aggelidis,P.; Teliousis,K.; Kaldrymidou,E.; Krey,G.; Sklaviadis,T.

TI Evaluation of the Possible Transmission of Prions to Sea Bass

QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Pathology and Pathogenesis P03.29

IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf

PT Konferenz-Poster

AB Transmissible spongiform encephalopathies (TSEs) are infectious neurodegenerative diseases in which the causative agent is thought to be PrPsc, an aberrant isoform of the normal cellular prion protein, PrPc. While TSEs have been studied extensively in mammals, very little is known about TSE pathogenesis in fish. As fish farming is an important industry that provides high protein nutrition for humans, both the prospect of a prion disease developing in fish and the possibility of farmed fish being contaminated with infectious mammalian PrPsc are of major concern.
We have undertaken a study with sea bass to evaluate the possibility of transmission of TSEs to fish. Two groups of sea bass were force fed with scrapie-infected sheep or BSE-infected bovine brain homogenates, while similar control populations were fed with normal brain homogenates. Following this challenge the inoculated fish were studied for clinical and behavioral signs of disease on a daily basis. At regular times during the post-inoculation period fish from each challenge group were sacrificed and their tissues subjected to histopathological examination, immunohistochemical detection of residual mammalian PrP and western blot analysis for detection of both mammalian and fish PrPs. The results from the first three years of this study show no indication that prion disease has been transmitted to sea bass. To demonstrate this more rigorously, a small group of seabass were rechallenged with scrapie brain homogenate after 3 years and monitored for a further 6 months. As well, we have used a cell culture system to evaluate the potential for in vitro conversion of recombinant fish PrP molecules to protease-K resistant isoforms in scrapie-infected N2a cells.

AD E. Salta, C. Panagiotidis, S. Petrakis, T. Sklaviadis, Centre for Research and Technology-Hellas, Institute of Agrobiotechology, Greece; E. Eleftheriadis, F. Arapoglou, G. Krey, National Agricultural Research Foundation, Fisheries Research Unit, Greece; D. Karagiannis, P. Aggelidis, K. Teliousis, E. Kaldrymidou, Aristotle University of Thessaloniki, School of Veterinary Medicine, Greece

SP englisch

PO Schottland

EA pdf-Datei und Poster (Autorenliste ergänzt um H. Schätzl)

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