Role of the highly conserved middle region of prion protein (PrP) in PrP-lipid interaction

Biochemistry

Volumn 49, Issue 37, 2010, Pages 8169-8176

  Wang, Fei ^a   Yin, Shaoman ^b   Wang, Xinhe ^a   Zha, Liang ^a   Sy, Man Sun ^b   Ma, Jiyan ^a  

^a OHIO STATE UNIVERSITY   (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; LIPIDS; POLYMORPHISM; SCANDIUM;

ANIONIC LIPIDS; DELETION MUTANTS; HYDROPHOBIC DOMAINS; ISOFORMS; LIPID BINDING; LYSINE RESIDUES; N-TERMINALS; POSITIVE CHARGES; POSITIVELY CHARGED; PRION DISEASE; PRION PROTEIN; PROTEINASE K;

HYDROPHOBICITY;

PRION PROTEIN; PROTEINASE K; ISOPROTEIN; PRION; PRNP PROTEIN, MOUSE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; GENE DELETION; GENE MUTATION; MOUSE; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN LOCALIZATION; PROTEIN POLYMORPHISM; ANIMAL; CHEMICAL PHENOMENA; CHEMISTRY; METABOLISM; PRION;

ANIMALS; ENDOPEPTIDASE K; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICE; PRIONS; PROTEIN ISOFORMS;

EID: 77956579315     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101146v     Document Type: Article

References (44)

1. Prusiner, S. B. (1998) Prions Proc. Natl. Acad. Sci. U.S.A. 95, 13363-13383
2. Caughey, B. and Chesebro, B. (1997) Prion protein and the transmissible spongiform encephalopathies Trends Cell Biol. 7, 56-62
3. Watts, J. C., Balachandran, A., and Westaway, D. (2006) The expanding universe of prion diseases PLoS Pathog. 2, e26
4. Collinge, J. (2001) Prion diseases of humans and animals: Their causes and molecular basis Annu. Rev. Neurosci. 24, 519-550
5. Aguzzi, A. (2006) Prion diseases of humans and farm animals: Epidemiology, genetics, and pathogenesis J. Neurochem. 97, 1726-1739
6. Caughey, B. and Baron, G. S. (2006) Prions and their partners in crime Nature 443, 803-810
7. Cohen, F. E. and Prusiner, S. B. (1998) Pathologic conformations of prion proteins Annu. Rev. Biochem. 67, 793-819
8. Baskakov, I. V. and Breydo, L. (2007) Converting the prion protein: What makes the protein infectious Biochim. Biophys. Acta 1772, 692-703
9. Collinge, J. and Clarke, A. R. (2007) A general model of prion strains and their pathogenicity Science 318, 930-936
10. Aguzzi, A., Baumann, F., and Bremer, J. (2008) The prions elusive reason for being Annu. Rev. Neurosci. 31, 439-477
11. Caughey, B., Baron, G. S., Chesebro, B., and Jeffrey, M. (2009) Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions Annu. Rev. Biochem. 78, 177-204
12. Wang, F., Wang, X., Yuan, C. G., and Ma, J. (2010) Generating a prion with bacterially expressed recombinant prion protein Science 327, 1132-1135
13. Supattapone, S. (2010) Biochemistry. What makes a prion infectious? Science 327, 1091-1092
14. Deleault, N. R., Lucassen, R. W., and Supattapone, S. (2003) RNA molecules stimulate prion protein conversion Nature 425, 717-720
15. Deleault, N. R., Geoghegan, J. C., Nishina, K., Kascsak, R., Williamson, R. A., and Supattapone, S. (2005) Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions J. Biol. Chem. 280, 26873-26879
16. Deleault, N. R., Harris, B. T., Rees, J. R., and Supattapone, S. (2007) Formation of native prions from minimal components in vitro Proc. Natl. Acad. Sci. U.S.A. 104, 9741-9746
17. Klein, T. R., Kirsch, D., Kaufmann, R., and Riesner, D. (1998) Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry Biol. Chem. 379, 655-666
18. Gabizon, R., McKinley, M. P., and Prusiner, S. B. (1987) Purified prion proteins and scrapie infectivity copartition into liposomes Proc. Natl. Acad. Sci. U.S.A. 84, 4017-4021
19. Baron, G. S., Magalhaes, A. C., Prado, M. A., and Caughey, B. (2006) Mouse-adapted scrapie infection of SN56 cells: Greater efficiency with microsome-associated versus purified PrP-res J. Virol. 80, 2106-2117
20. Taraboulos, A., Scott, M., Semenov, A., Avrahami, D., Laszlo, L., and Prusiner, S. B. (1995) Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform J. Cell Biol. 129, 121-132
21. Naslavsky, N., Shmeeda, H., Friedlander, G., Yanai, A., Futerman, A. H., Barenholz, Y., and Taraboulos, A. (1999) Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions J. Biol. Chem. 274, 20763-20771
22. Baron, G. S. and Caughey, B. (2003) Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform J. Biol. Chem. 278, 14883-14892
23. Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein J. Biol. Chem. 274, 36859-36865
24. Sanghera, N. and Pinheiro, T. J. (2002) Binding of prion protein to lipid membranes and implications for prion conversion J. Mol. Biol. 315, 1241-1256
25. Kazlauskaite, J., Sanghera, N., Sylvester, I., Venien-Bryan, C., and Pinheiro, T. J. (2003) Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization Biochemistry 42, 3295-3304
26. Critchley, P., Kazlauskaite, J., Eason, R., and Pinheiro, T. J. (2004) Binding of prion proteins to lipid membranes Biochem. Biophys. Res. Commun. 313, 559-567
27. Luhrs, T., Zahn, R., and Wuthrich, K. (2006) Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions J. Mol. Biol. 357, 833-841
28. C Proc. Natl. Acad. Sci. U.S.A. 105, 10815-10819
29. Wang, F., Yang, F., Hu, Y., Wang, X., Jin, C., and Ma, J. (2007) Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions Biochemistry 46, 7045-7053
30. Yin, S., Pham, N., Yu, S., Li, C., Wong, P., Chang, B., Kang, S. C., Biasini, E., Tien, P., Harris, D. A., and Sy, M. S. (2007) Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans Proc. Natl. Acad. Sci. U.S.A. 104, 7546-7551
31. Zahn, R., von Schroetter, C., and Wuthrich, K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding FEBS Lett. 417, 400-404
32. Yin, S. M., Zheng, Y., and Tien, P. (2003) On-column purification and refolding of recombinant bovine prion protein: Using its octarepeat sequences as a natural affinity tag Protein Expression Purif. 32, 104-109
33. Wang, X., Wang, F., Arterburn, L., Wollmann, R., and Ma, J. (2006) The interaction between cytoplasmic prion protein and the hydrophobic lipid core of membrane correlates with neurotoxicity J. Biol. Chem. 281, 13559-13565
34. Polymenidou, M., Stoeck, K., Glatzel, M., Vey, M., Bellon, A., and Aguzzi, A. (2005) Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease Lancet Neurol. 4, 805-814
35. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., and Wuthrich, K. (1996) NMR structure of the mouse prion protein domain PrP(121-321) Nature 382, 180-182
36. Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wuthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231) FEBS Lett. 413, 282-288 (Pubitemid 27353285)
37. Ironside, J. W., Ritchie, D. L., and Head, M. W. (2005) Phenotypic variability in human prion diseases Neuropathol. Appl. Neurobiol. 31, 565-579
38. Cobb, N. J., Sonnichsen, F. D., McHaourab, H., and Surewicz, W. K. (2007) Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure Proc. Natl. Acad. Sci. U.S.A. 104, 18946-18951
39. Hegde, R. S., Mastrianni, J. A., Scott, M. R., DeFea, K. A., Tremblay, P., Torchia, M., DeArmond, S. J., Prusiner, S. B., and Lingappa, V. R. (1998) A transmembrane form of the prion protein in neurodegenerative disease Science 279, 827-834
40. Aguzzi, A., Sigurdson, C., and Heikenwaelder, M. (2008) Molecular mechanisms of prion pathogenesis Annu. Rev. Pathol. 3, 11-40
41. Telling, G. C., Haga, T., Torchia, M., Tremblay, P., DeArmond, S. J., and Prusiner, S. B. (1996) Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice Genes Dev. 10, 1736-1750
42. Yamada, M., Itoh, Y., Inaba, A., Wada, Y., Takashima, M., Satoh, S., Kamata, T., Okeda, R., Kayano, T., Suematsu, N., Kitamoto, T., Otomo, E., Matsushita, M., and Mizusawa, H. (1999) An inherited prion disease with a PrP P105L mutation: Clinicopathologic and PrP heterogeneity Neurology 53, 181-188
43. Collins, S., McLean, C. A., and Masters, C. L. (2001) Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, and kuru: A review of these less common human transmissible spongiform encephalopathies J. Clin. Neurosci. 8, 387-397
44. Hosszu, L. L., Jackson, G. S., Trevitt, C. R., Jones, S., Batchelor, M., Bhelt, D., Prodromidou, K., Clarke, A. R., Waltho, J. P., and Collinge, J. (2004) The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC J. Biol. Chem. 279, 28515-28521