그리스 과학자들이 물고기도 광우병에 걸릴 수 있다는 연구결과를 최근 PLoS ONE 4(7)에 발표하였습니다.
Evgenia Salta박사팀은 그리스의 대표적인 양식 물고기인 치푸라(gilthead sea bream=Sparus aurata)에게 BSE 및 스크래피를 경구로 감염시킨 결과, 24개월 후에 물고기의 뇌에 비정형 프리온 단백질이 침착된 것을 항체검사를 통해 확인하였습니다.(정상 프리온 단백질을 프로테인키나제라는 효소로 처리한 후 항체검사를 통해 비정형 프리온 단백질을 검출했습니다.)
그런데 이 물고기들은 신경퇴행 등의 임상증상을 보이지는 않았다고 합니다.
그리고 스크래피에 감염된 양의 뇌를 경구로 투여한 물고기보다 BSE에 감염된 소의 뇌를 경구로 투여한 물고기에서 더 빨리 그리고 더 광범위하게 비정형 프리온이 축적되었다고 합니다.
양식 물고기 같은 경우는 많은 대중들의 식단에 올라가는 식재료이기 때문에 물고기의 광우병에 대한 추가 연구가 필요할 뿐만 아니라, 물고기를 통한 인간광우병 전염 가능성에 대한 경각심을 가져야 할 것입니다.
Evgenia Salta박사팀의 연구결과에 대한 요약문은 아래에 있으며, 전문은 첨부파일을 보시면 됩니다.
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Evaluation of the Possible Transmission of BSE and Scrapie to Gilthead Sea Bream (Sparus aurata)
출처 : PLoS ONE 4(7): e6175. doi:10.1371/journal.pone.0006175
Received: March 27, 2009; Accepted: May 19, 2009; Published: July 28, 2009
http://www.plosone.org/article/info:doi%2F10.1371%2Fjournal.pone.0006175
1 Department of Pharmacology, Aristotle University of Thessaloniki, Thessaloniki, Greece, 2 Centre for Research and Technology-Hellas, Institute of Agrobiotechnology, Thessaloniki, Greece, 3 Laboratory of Pathology, School of Veterinary Medicine, Aristotle University of Thessaloniki, Thessaloniki, Greece, 4 Max Delbruck Center for Molecular Medicine, Department of Neuroproteomics, Berlin-Buch, Germany, 5 National Agricultural Research Foundation, Fisheries Research Institute, Nea Peramos, Greece, 6 B’ Department of Neurology, AHEPA University Hospital, Aristotle University of Thessaloniki, Thessaloniki, Greece, 7 Department of Business Administration, University of Macedonia, Thessaloniki, Greece
Abstract
In transmissible spongiform encephalopathies (TSEs), a group of fatal neurodegenerative disorders affecting many species, the key event in disease pathogenesis is the accumulation of an abnormal conformational isoform (PrPSc) of the host-encoded cellular prion protein (PrPC). While the precise mechanism of the PrPC to PrPSc conversion is not understood, it is clear that host PrPC expression is a prerequisite for effective infectious prion propagation. Although there have been many studies on TSEs in mammalian species, little is known about TSE pathogenesis in fish. Here we show that while gilthead sea bream (Sparus aurata) orally challenged with brain homogenates prepared either from a BSE infected cow or from scrapie infected sheep developed no clinical prion disease, the brains of TSE-fed fish sampled two years after challenge did show signs of neurodegeneration and accumulation of deposits that reacted positively with antibodies raised against sea bream PrP. The control groups, fed with brains from uninfected animals, showed no such signs. Remarkably, the deposits developed much more rapidly and extensively in fish inoculated with BSE-infected material than in the ones challenged with the scrapie-infected brain homogenate, with numerous deposits being proteinase K-resistant. These plaque-like aggregates exhibited congophilia and birefringence in polarized light, consistent with an amyloid-like component. The neurodegeneration and abnormal deposition in the brains of fish challenged with prion, especially BSE, raises concerns about the potential risk to public health. As fish aquaculture is an economically important industry providing high protein nutrition for humans and other mammalian species, the prospect of farmed fish being contaminated with infectious mammalian PrPSc, or of a prion disease developing in farmed fish is alarming and requires further evaluation.
