Prion strain mutation determined by prion protein conformational compatibility and primary structure

Science

Volumn 328, Issue 5982, 2010, Pages 1154-1158

  Angers, Rachel C ^a,h   Kang, Hae Eun ^a   Napier, Dana ^a   Browning, Shawn ^a,i   Seward, Tanya ^a   Mathiason, Candace ^b   Balachandran, Aru ^c   McKenzie, Debbie ^d   Castilla, Joaquín ^e   Soto, Claudio ^f   Jewell, Jean ^g   Graham, Catherine ^c   Hoover, Edward A ^b   Telling, Glenn C ^a  

^a UNIVERSITY OF KENTUCKY MEDICAL CENTER   (United States)

^b Department of Environmental and Radiological Health Sciences   (United States)

^c CANADIAN FOOD INSPECTION AGENCY   (Canada)

^d UNIVERSITY OF ALBERTA   (Canada)

^e BASQUE FOUNDATION FOR SCIENCE   (Spain)

^f UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^g UNIVERSITY OF WYOMING   (United States)

^h MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

ⁱ SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID; PRION PROTEIN;

DISEASE TRANSMISSION; EPIDEMIC; GENETICALLY MODIFIED ORGANISM; MUTATION; NUCLEIC ACID; PRION DISEASE; PROTEIN; RODENT;

AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; BRAIN; CHRONIC WASTING DISEASE; DEER; IMMUNOHISTOCHEMISTRY; MOUSE; NONHUMAN; PRION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; TRANSGENIC MOUSE;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; BRAIN CHEMISTRY; DEER; DISEASE SUSCEPTIBILITY; MICE; MICE, TRANSGENIC; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PRPC PROTEINS; PRPSC PROTEINS; SELECTION, GENETIC; SERIAL PASSAGE; SPECIES SPECIFICITY; WASTING DISEASE, CHRONIC;

CERVIDAE; MUS MUSCULUS;

EID: 77952964383     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1187107     Document Type: Article

References (32)

1. R. A. Bessen, R. F. Marsh, J. Virol. 68, 7859 (1994).
2. G. C. Telling et al., Science 274, 2079 (1996).
3. J. Collinge, K. C. L. Sidle, J. Meads, J. Ironside, A. F. Hill, Nature 383, 685 (1996).
4. D. Peretz et al., Protein Sci. 10, 854 (2001).
5. K. M. Green et al., PLoS Pathog. 4, e1000139 (2008).
6. M. E. Bruce, A. G. Dickinson, J. Gen. Virol. 68, 79 (1987).
7. J. C. Bartz, R. F. Marsh, D. I. McKenzie, J. M. Aiken, Virology 251, 297 (1998).
8. S. R. Browning et al., J. Virol. 78, 13345 (2004).
9. G. LaFauci et al., J. Gen. Virol. 87, 3773 (2006).
10. G. Tamgüney et al., J. Virol. 80, 9104 (2006).
11. J. D. F. Wadsworth et al., Science 306, 1793 (2004); published online 11 November 2004 (10.1126/ science. 1103932).
12. K. M. Green et al., J. Gen. Virol. 89, 598 (2008).
13. R. C. Angers et al., Science 311, 1117 (2006); published online 26 January 2006 (10.1126/science.1122864).
14. R. C. Angers et al., Emerg. Infect. Dis. 15, 696 (2009).
15. A. G. Dickinson, V. M. H. Meikle, Mol. Gen. Genet. 112, 73 (1971).
16. M. E. Bruce, A. G. Dickinson, in Slow Transmissible Diseases of the Nervous System, Vol. 2, S. B. Prusiner, W. J. Hadlow, Eds. (Academic Press, New York, 1979), pp. 71-86.
17. M. E. Bruce, P. A. McBride, C. F. Farquhar, Neurosci. Lett. 102, 1 (1989).
18. Materials and methods are available as supporting material on Science Online.
19. H. Fraser, A. G. Dickinson, ;. Comp. Pathol. 78, 301 (1968).
20. A. Taraboulos et al., Proc. Natl. Acad. Sci. USA 89, 7620 (1992).
21. M. E. Bruce, H. Fraser, Acta Neuropathol. 58, 133 (1982).
22. J. Castilla, P. Saá, C. Hetz, C. Soto, Cell 121, 195 (2005).
23. J. Li, S. Browning, S. P. Mahal, A. M. Oelschlegel, C. Weissmann, Science 327, 869 (2010); published online 31 December 2009 (10.1126/science.1183218).
24. G. Legname et al., Proc. Nati Acad. Sci. USA 103, 19105 (2006).
25. M. Polymenidou et al., Lancet Neurol. 4, 805 (2005).
26. J. Collinge, Lancet 354, 317 (1999).
27. J. Collinge, A. R. Clarke, Science 318, 930 (2007).
28. C. J. Sigurdson et al., J. Virol. 80, 12303 (2006).
29. G. J. Raymond et al., J. Virol. 81, 4305 (2007).
30. C. Johnson et al., J. Gen. Virol. 87, 2109 (2006).
31. Q. Kong et al., J. Neurosci. 25, 7944 (2005).
32. We thank Prionics for mAb 6H4, V. Saylor for technical help, A. Aguzzi for mAb POM2, P. Nelson for neuropathological expertise, R. Kryscio and J. Marcum for biostatistical advice, and C. Ryou for reading the manuscript. CS. is currently Founder and Chief Scientific Officer of Amprion Inc., a privately held company focusing on exploiting PMCA for sensitive detection of prions and early disease diagnosis. These studies were supported by grant 2RO1 NS040334-04 from the National Institute of Neurological Disorders and Stroke, grants N01-AI-25491 and 1P01AI077774-01 from the National Institute of Allergy and Infectious Diseases, and grant V180003 from the U.S. Department of Defense. R.C.A. and S.B. were supported by T32 DA022738 and T32 AI49795 Training Programs from the National Institute on Drug Abuse and the National Institute of Allergy and Infectious Diseases, respectively.