Conversion of bacterially expressed recombinant prion protein

Methods

Volumn 53, Issue 3, 2011, Pages 208-213

  Wang, Fei ^a   Wang, Xinhe ^a   Ma, Jiyan ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

In vitro conversion; Infectivity; Neurodegeneration; Prion; Recombinant protein

Indexed keywords

PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEGENERATIVE DISEASE; FEMALE; INFECTION; MOUSE; NERVE DEGENERATION; NONHUMAN; PATHOGENESIS; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION;

ANIMALS; BRAIN; CLONING, MOLECULAR; DISEASE MODELS, ANIMAL; ENDOPEPTIDASE K; ESCHERICHIA COLI; FEMALE; MICE; PHOSPHATIDYLGLYCEROLS; PRION DISEASES; PROTEIN FOLDING; PRPC PROTEINS; PRPSC PROTEINS; RECOMBINANT PROTEINS; RNA; SONICATION;

MUS;

EID: 79952187533     PISSN: 10462023     EISSN: 10959130     Source Type: Journal    
DOI: 10.1016/j.ymeth.2010.12.013     Document Type: Article

References (28)

1. Prusiner S.B. Prions. Proc Natl Acad Sci USA 1998, 95:13363-13383.
2. Weissmann C. Molecular biology of prion disease. Trends in Cell Biol. 1994, 4:10.
3. Aguzzi A., Heppner F.L. Pathogenesis of prion diseases: a progress report. Cell Death Differ 2000, 7:889-902.
4. Cohen F.E., Prusiner S.B. Pathologic conformations of prion proteins. Annu Rev Biochem 1998, 67:793-819.
5. Aguzzi A., Baumann F., Bremer J. The prion's elusive reason for being. Annu Rev Neurosci 2008, 31:439-477.
6. Caughey B., Baron G.S., Chesebro B., Jeffrey M. Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 2009, 78:177-204.
7. Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T., Caughey B. Cell-free formation of protease-resistant prion protein. Nature 1994, 370:471-474.
8. Saborio G.P., Permanne B., Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001, 411:810-813.
9. Castilla J., Saa P., Hetz C., Soto C. In vitro generation of infectious scrapie prions. Cell 2005, 121:195-206.
10. Baron G.S., Caughey B. Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J Biol Chem 2003, 278:14883-14892.
11. Deleault N.R., Lucassen R.W., Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003, 425:717-720.
12. Deleault N.R., Geoghegan J.C., Nishina K., Kascsak R., Williamson R.A., Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J Biol Chem 2005, 280:26873-26879.
13. Deleault N.R., Harris B.T., Rees J.R., Supattapone S. From the cover: formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 2007, 104:9741-9746.
14. Wang F., Yang F., Hu Y., Wang X., Jin C., Ma J. Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 2007, 46:7045-7053.
15. Wang F., Wang X., Yuan C.G., Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010, 327:1132-1135.
16. Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-321). Nature 1996, 382:180-182.
17. Riek R., Hornemann S., Wider G., Glockshuber R., Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 1997, 413:282-288.
18. Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E., Prusiner S.B., Wright P.E., Dyson H.J. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 1997, 94:13452-13457.
19. Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Lopez Garcia F., Billeter M., Calzolai L., Wider G., Wuthrich K. NMR solution structure of the human prion protein. Proc Natl Acad Sci USA 2000, 97:145-150.
20. Lopez Garcia F., Zahn R., Riek R., Wuthrich K. NMR structure of the bovine prion protein. Proc Natl Acad Sci USA 2000, 97:8334-8339.
21. Jackson G.S., Hosszu L.L., Power A., Hill A.F., Kenney J., Saibil H., Craven C.J., Waltho J.P., Clarke A.R., Collinge J. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 1999, 283:1935-1937.
22. Baskakov I.V., Legname G., Prusiner S.B., Cohen F.E. Folding of prion protein to its native alpha-helical conformation is under kinetic control. J Biol Chem 2001, 276:19687-19690.
23. Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., Cohen F.E. Pathway complexity of prion protein assembly into amyloid. J Biol Chem 2002, 277:21140-21148.
24. Leffers K.W., Wille H., Stohr J., Junger E., Prusiner S.B., Riesner D. Assembly of natural and recombinant prion protein into fibrils. Biol Chem 2005, 386:569-580.
25. Luhrs T., Zahn R., Wuthrich K. Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions. J Mol Biol 2006, 357:833-841.
26. Hornemann S., Schorn C., Wuthrich K. NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep 2004, 5:1159-1164.
27. Zahn R., von Schroetter C., Wuthrich K. Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett 1997, 417:400-404.
28. Polymenidou M., Stoeck K., Glatzel M., Vey M., Bellon A., Aguzzi A. Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. Lancet Neurol 2005, 4:805-814.