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

Author

Listed:
  • 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
    Massachusetts Institute of Technology)

  • 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
    ☆Center for Neurological Diseases, Brigham & Womens Hospital, Harvard Medical School)

  • Byron Caughey

    (*Rocky Mountain Laboratories, NIAID, National Institutes of Health)

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.

Suggested Citation

  • 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 & Ric, 1997. "Molecular assessment of the potential transmissibilities of BSE and scrapie to humans," Nature, Nature, vol. 388(6639), pages 285-288, July.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6639:d:10.1038_40876
    DOI: 10.1038/40876
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