Molecular assessment of the potential transmissibilities of BSE and scrapie to humans

Gregory J. Raymond, James Hope, David A. Kocisko, Suzette A. Priola, Lynne D. Raymond, Alex Bossers, James Ironside (), Robert G. Will, Shu G. Chen, Robert B. Petersen, Pierluigi Gambetti, Richard Rubenstein, Mari A. Smits, Peter T. Lansbury and Byron Caughey ()
Additional contact information
Gregory J. Raymond: *Rocky Mountain Laboratories, NIAID, National Institutes of Health
James Hope: †BBSRC Institute for Animal Health, Compton Laboratory, Compton
David A. Kocisko: *Rocky Mountain Laboratories, NIAID, National Institutes of Health
Suzette A. Priola: *Rocky Mountain Laboratories, NIAID, National Institutes of Health
Lynne D. Raymond: *Rocky Mountain Laboratories, NIAID, National Institutes of Health
Alex Bossers: DLO-Institute for Animal Science and Health
James Ironside: ‖Western General Hospital, CJD Surveillance Unit
Robert G. Will: ‖Western General Hospital, CJD Surveillance Unit
Shu G. Chen: ¶Case Western Reserve University, Institute of Pathology
Robert B. Petersen: ¶Case Western Reserve University, Institute of Pathology
Pierluigi Gambetti: ¶Case Western Reserve University, Institute of Pathology
Richard Rubenstein: #NYS Institute for Basic Research
Mari A. Smits: DLO-Institute for Animal Science and Health
Peter T. Lansbury: Massachusetts Institute of Technology
Byron Caughey: *Rocky Mountain Laboratories, NIAID, National Institutes of Health

Nature, 1997, vol. 388, issue 6639, 285-288

Abstract: Abstract More than a million cattle infected with bovine spongiform encephalopathy (BSE) may have entered the human food chain1. Fears that BSE might transmit to man were raised when atypical cases of Creutzfeldt–Jakob disease (CJD), a human transmissible spongiform encephalopathy (TSE), emerged in the UK2,3. In BSE and other TSE diseases, the conversion of the protease-sensitive host prion protein (PrP-sen) to a protease-resistant isoform (PrP-res) is an important event in pathogenesis4,5,6,7. Biological aspects of TSE diseases are reflected in the specificities of in vitro PrP conversion reactions8,9,10,11,12. Here we show that there is a correlation between in vitro conversion efficiencies and known transmissibilities of BSE, sheep scrapie and CJD. On this basis, we used an in vitro system to gauge the potential transmissibility of scrapie and BSE to humans. We found limited conversion of human PrP-sen to PrP-res driven by PrP-res associated with both scrapie (PrPSc) and BSE (PrPBSE). The efficiencies of these heterologous conversion reactions were similar but much lower than those of relevant homologous conversions. Thus the inherent ability of these infectious agents of BSE and scrapie to affect humans following equivalent exposure may be finite but similarly low.

Date: 1997
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DOI: 10.1038/40876

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