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

Nature

Volumn 388, Issue 6639, 1997, Pages 285-288

  Raymonds, Gregory J ^a   Hope, James ^b   Kocisko, David A ^a,b   Priola, Suzette A ^a   Raymond, Lynne D ^a   Bossers, Alex ^d   Ironside, James ^e   Will, Robert G ^e   Chen, Shu G ^f   Petersen, Robert B ^f   Gambetti, Pierluigi ^f   Rubenstein, Richard ^g   Smits, Mari A ^d   Lansbury Jr , Peter T ^c,h   Caughey, Byron ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b INSTITUTE FOR ANIMAL HEALTH   (United Kingdom)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d WAGENINGEN UNIVERSITY   (Netherlands)

^e WESTERN GENERAL HOSPITAL   (United Kingdom)

^f CASE WESTERN RESERVE UNIVERSITY   (United States)

^g NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

^h BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; METHIONINE; PRION PROTEIN; PROTEINASE; SULFUR 35; VALINE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; AUTORADIOGRAPHY; BOVINE SPONGIFORM ENCEPHALOPATHY; CATTLE; CREUTZFELDT JAKOB DISEASE; FOOD CHAIN; GENOTYPE; GLYCOSYLATION; HAMSTER; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SCRAPIE; SHEEP;

ANIMALS; CATTLE; CELL-FREE SYSTEM; CREUTZFELDT-JAKOB SYNDROME; CRICETINAE; DISEASE SUSCEPTIBILITY; ENCEPHALOPATHY, BOVINE SPONGIFORM; ENDOPEPTIDASE K; HUMANS; MESOCRICETUS; MICE; NERVE TISSUE PROTEINS; PRIONS; PRPC PROTEINS; PRPSC PROTEINS; SCRAPIE; SHEEP; SPECIES SPECIFICITY; TUMOR CELLS, CULTURED; ZOONOSES;

ANIMALIA; BOS TAURUS; BOVINAE; CRICETINAE; OVIS ARIES;

EID: 0030802361     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/40876     Document Type: Article

References (26)

1. Andersen, R. M. et al. Transmission dynamics and epidemiology of BSE in British cattle. Nature 382, 779-788(1996).
2. Will, R. G. et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925 (1996).
3. Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J. & Hill, A. F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383, 685-690 (1996).
4. Hope, J. et al. Fibrils from brains of cows with new cattle disease contain scrapie-associated protein. Nature 336, 390-392 (1988).
5. Bolton, D. C., McKinley, M. P. & Prusiner, S. B. Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311 (1982).
6. Weissmann, C. Molecular biology of transmissible spongiform encephalopathies. FEBS Lett. 389, 3-11 (1996).
7. Caughey, B. & Chesebro, B. Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol. 7, 56-62 (1997).
8. Kocisko, D. A. et al. Cell-free formation of protease-resistant prion protein. Nature 370, 471-474 (1994).
9. Kocisko, D. A. et al. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier Proc. Natl Acad. Sci. USA 92, 3923-3927 (1995).
10. Bessen, R. A. et al. Non-genetic propagation of strain-specific phenotypes of scrapie prion protein. Nature 375, 698-700 (1995).
11. Bossers, A. et al. Scrapie susceptivility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms. Proc. Natl Acad. Sci. USA 94, 4931-4936 (1997).
12. Bessen, R. A., Raymond, G. J. & Caughey, B. In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices. J. Biol. Chem. 272, 15227-15231 (1997).
13. Fraser, H., McConnell, I., Wells, G. A. H. & Dawson, M. Transmission of bovine spongiform encephalopathy to mice. Vet. Rec. 123, 472 (1988).
14. Dawson, M., Wells, G. A. H. & Parker, B. N. J. Preliminary evidence of the experimental transmissibility of bovine spongiform encephalopathy to cattle. Vet Rec. 126, 112-113 (1990).
15. Foster, J. D., Hope, J. & Fraser, H. Transmission of bovine spongiform encephalopathy to sheep and goats. Vet. Rec. 133, 339-341 (1993).
16. Goldmann, W., Hunter, N., Smith, G., Foster, I. & Hope, J. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75, 989-995 (1994).
17. Caughey, B., Kocisko, D. A., Raymond, G. J. & Lansbury, P. T. Aggregates of scrapie associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2, 807-817 (1995),
18. Palmer, M. S., Dryden, A. J., Hughes, J. T. & Collinge, J. Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352, 340-342 (1991).
19. Riek, R. et al. NMR structure of the mouse prion protein domain PrP( 121-231). Nature 382, 180-182 (1996).
20. Collinge, J. et al. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 378, 779-783 (1995).
21. Hope, J. et al. The major polypeptide of scrapie-associated fibrils (SAP) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J. 5, 2591-2597 (1986).
22. van Keulen, L. J. M. et al. Immunohistochemical detection and localization of prion protein in brain : tissue of sheep with natural scrapie. Vet. Pathol. 32, 299-308 (1995).
23. Kascsak, R. J. et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61, 3688-3693 (1987).
24. Petersen, R. B., Parchi, P., Richardson, S. L., Urig, C. B. & Gambetti, P. Effect of the D178N mutation andthecodon 129 polymorphism on the metabolism of the prion protein. J. Biol Chem. 271, 12661-12668 (1996).
25. Caughey, B. et al. in Prion Diseases (eds Baker, H. F. Ridley, R. M.) 285-300 (Humana, Totowa, 1996).
26. Caughey, B., Raymond, G. J., Kocisko, D. A. & Lansbury, P. T. Jr Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J. Virol. 71, 4107-4110 (1997).