The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro

FEBS Letters

Volumn 583, Issue 22, 2009, Pages 3671-3675

  Kim, Jae Il ^a   Surewicz, Krystyna ^a   Gambetti, Pierluigi ^a   Surewicz, Witold K ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Conformational conversion; Glycophosphatidylinositol anchor; Prion; Prion protein; Transmissible spongiform encephalopathy

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; PRION PROTEIN; RECOMBINANT PROTEIN;

ANIMAL TISSUE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GENE AMPLIFICATION; GENE CONVERSION; IMMUNODETECTION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; SCRAPIE;

ANIMALS; BLOTTING, WESTERN; BRAIN; CRICETINAE; GLYCOSYLPHOSPHATIDYLINOSITOLS; MESOCRICETUS; MICE; MICE, KNOCKOUT; PROTEIN FOLDING; PRPC PROTEINS; PRPSC PROTEINS; RECOMBINANT PROTEINS; SCRAPIE;

EID: 71749087690     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.049     Document Type: Article

References (27)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA 95 (1998) 13363-13383
2. Caughey B., Baron G.S., Chesebro B., and Jeffrey M. Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions. Annu. Rev. Biochem. 78 (2009) 177-204
3. Cobb N.J., and Surewicz W.K. Prion diseases and their biochemical mechanisms. Biochemistry 48 (2009) 2574-2585
4. Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T., and Caughey B. Cell-free formation of protease-resistant prion protein. Nature 370 (1994) 471-474
5. Hill A.F., Antoniou M., and Collinge J. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80 Pt 1 (1999) 11-14
6. Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
7. Castilla J., Saa P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
8. Castilla J., Gonzalez-Romero D., Saa P., Morales R., De Castro J., and Soto C. Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions. Cell 134 (2008) 757-768
9. Castilla J., Morales R., Saa P., Barria M., Gambetti P., and Soto C. Cell-free propagation of prion strains. EMBO J. 27 (2008) 2557-2566
10. Deleault N.R., Harris B.T., Rees J.R., and Supattapone S. Formation of native prions from minimal components in vitro. Proc. Natl. Acad. Sci. USA 104 (2007) 9741-9746
11. Morillas M., Swietnicki W., Gambetti P., and Surewicz W.K. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274 (1999) 36859-36865
12. Smirnovas V., Kim J.I., Lu X., Atarashi R., Caughey B., and Surewicz W.K. Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by H/D exchange. J. Biol. Chem. 284 (2009) 24233-24241
13. Nishina K.A., and Supattapone S. Immunodetection of glycophosphatidylinositol-anchored proteins following treatment with phospholipase C. Anal. Biochem. 363 (2007) 318-320
14. Deleault N.R., Lucassen R.W., and Supattapone S. RNA molecules stimulate prion protein conversion. Nature 425 (2003) 717-720
15. Bieschke J., Weber P., Sarafoff N., Beekes M., Giese A., and Kretzschmar H. Autocatalytic self-propagation of misfolded prion protein. Proc. Natl. Acad. Sci. USA 101 (2004) 12207-12211
16. Hornemann S., Schorn C., and Wuthrich K. NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep. 5 (2004) 1159-1164
17. Piro J.R., Harris B.T., Nishina K., Soto C., Morales R., Rees J.R., and Supattapone S. Prion protein glycosylation is not required for strain-specific neurotropism. J. Virol. 83 (2009) 5321-5328
18. Stahl N., Borchelt D.R., Hsiao K., and Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51 (1987) 229-240
19. Atarashi R., Moore R.A., Sim V.L., Hughson A.G., Dorward D.W., Onwubiko H.A., Priola S.A., and Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Methods 4 (2007) 645-650
20. Baron G.S., Wehrly K., Dorward D.W., Chesebro B., and Caughey B. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J. 21 (2002) 1031-1040
21. Kirby L., Birkett C.R., Rudyk H., Gilbert I.H., and Hope J. In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion. J. Gen. Virol. 84 (2003) 1013-1020
22. Caughey B. Prion protein interconversions. Philos. Trans. R. Soc. Lond. B, Biol. Sci. 356 (2001) 197-200 [discussion 200-202]
23. Caughey B., and Raymond G.J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266 (1991) 18217-18223
24. McNally K.L., Ward A.E., and Priola S.A. Cells expressing anchorless prion protein are resistant to scrapie infection. J. Virol. 83 (2009) 4469-4475
25. Chesebro B., et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308 (2005) 1435-1439
26. Xiao X., et al. Failure to detect the presence of prions in the uterine and gestational tissues from a Gravida with Creutzfeldt-Jakob disease. Am. J. Pathol. 174 (2009) 1602-1608
27. Gregori L., Kovacs G.G., Alexeeva I., Budka H., and Rohwer R.G. Excretion of transmissible spongiform encephalopathy infectivity in urine. Emerg. Infect. Dis. 14 (2008) 1406-1412