Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrPc to PrPSc in prion-infected neuroblastoma cells

Journal of Virology

Volumn 86, Issue 10, 2012, Pages 5626-5636

  Hara, Hideyuki ^a   Okemoto Nakamura, Yuko ^a   Shinkai Ouchi, Fumiko ^a   Hanada, Kentaro ^a   Yamakawa, Yoshio ^a   Hagiwara, Ken'ichi ^a  

^a NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; MINICHROMOSOME MAINTENANCE PROTEIN 2; PRION PROTEIN; PRION PROTEIN ANTIBODY; PROTEIN P8;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHIMERA; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REGULATION; GENE CONVERSION; MOUSE; NEUROBLASTOMA CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CHICKENS; HUMANS; MICE; MOLECULAR SEQUENCE DATA; NEUROBLASTOMA; PRION DISEASES; PRIONS; PRPC PROTEINS; PRPSC PROTEINS; SEQUENCE ALIGNMENT;

EID: 84861309388     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.06606-11     Document Type: Article

References (54)

1. Sc replicative interface. J. Biol. Chem. 283:34021-34028.
2. Butler DA, et al. 1988. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J. Virol. 62:1558-1564.
3. Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. 2005. Prion protein NMR structures of chickens, turtles, and frogs. Proc. Natl. Acad. Sci. U. S. A. 102:651-655.
4. Caughey BW, et al. 1991. Secondary structure analysis of the scrapieassociated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30:7672-7680.
5. Chabry J, Caughey B, Chesebro B. 1998. Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J. Biol. Chem. 273:13203-13207.
6. Chesebro B, et al. 1985. Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain. Nature 315:331-333.
7. Choi JK, et al. 2006. Generation of monoclonal antibody recognized by the GXXXG motif (glycine zipper) of prion protein. Hybridoma 25:271-277.
8. DebBurman SK, Raymond GJ, Caughey B, Lindquist S. 1997. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. U. S. A. 94:13938-13943.
9. DeMarco ML, Daggett V. 2004. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. U. S. A. 101: 2293-2298.
10. DeMarco ML, Silveira J, Caughey B, Daggett V. 2006. Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry 45:15573-15582.
11. Donne DG, et al. 1997. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. U. S. A. 94:13452-13457.
12. Enari M, Flechsig E, Weissmann C. 2001. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl. Acad. Sci. U. S. A. 98:9295-9299.
13. Flechsig E, et al. 2000. Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 27:399-408.
14. Flechsig E, Weissmann C. 2004. The role of PrP in health and disease. Curr. Mol. Med. 4:337-353.
15. Govaerts C, Wille H, Prusiner SB, Cohen FE. 2004. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Acad. Sci. U. S. A. 101:8342-8347.
16. Harrison CF, et al. 2010. Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity. J. Biol. Chem. 285:20213-20223.
17. Hetz C, Maundrell K, Soto C. 2003. Is loss of function of the prion protein the cause of prion disorders? Trends. Mol. Med. 9:237-243.
18. Horiuchi M, Caughey B. 1999. Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J. 18:3193-3203.
19. Horiuchi M, Priola SA, Chabry J, Caughey B. 2000. Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriers. Proc. Natl. Acad. Sci. U. S. A. 97:5836-5841.
20. Hsiao K, et al. 1989. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 338:342-345.
21. Kaneko K, et al. 1997. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. U. S. A. 94:10069-10074.
22. Kim CL, et al. 2004. Antigenic characterization of an abnormal isoform of prion protein using a new diverse panel of monoclonal antibodies. Virology 320:40-51.
23. Sc replication in vitro. Amyloid 11:14-20.
24. Kitamoto T, et al. 1993. A new inherited prion disease (PrP-P105L mutation) showing spastic paraparesis. Ann. Neurol. 34:808-813.
25. Kong Q, et al. 2004. Inherited prion diseases, p 673-775. In Prusiner SB (ed), Prion biology and diseases, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
26. Kunes KC, Clark SC, Cox DL, Singh RR. 2008. Left handed β helix models for mammalian prion fibrils. Prion 2:81-90.
27. Leclerc E, et al. 2001. Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J. 20:1547-1554.
28. Lund C, Olsen CM, Tveit H, Tranulis MA. 2007. Characterization of the prion protein 3F4 epitope and its use as a molecular tag. J. Neurosci. Methods 165:183-190.
29. Moroncini G, et al. 2004. Motif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPSc. Proc. Natl. Acad. Sci. U. S. A. 101:10404-10409.
30. Moroncini G, et al. 2006. Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antibody. Neurobiol. Dis. 23:717-724.
31. Nelson R, et al. 2005. Structure of the cross-β spine of amyloid-like fibrils. Nature 435:773-778.
32. Oesch B, et al. 1985. A cellular gene encodes scrapie PrP 27-30 protein. Cell 40:735-746.
33. Okemoto-Nakamura Y, et al. 2008. Synthetic fibril peptide promotes clearance of scrapie prion protein by lysosomal degradation. Microbiol. Immunol. 52:357-365.
34. Peretz D, et al. 1997. A conformational transition at theNterminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273:614-622.
35. Peretz D, et al. 2001. Antibodies inhibit prion propagation and clear cultures of prion infectivity. Nature 412:739-743.
36. Premzl M, Gamulin V. 2007. Comparative genomic analysis of prion genes. BMC Genomics 8:1.
37. Priola SA, Chesebro B. 1995. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69:7754-7758.
38. Priola SA, Lawson VA. 2001. Glycosylation influences cross-species formation of protease-resistant prion protein. EMBO J. 20:6692-6699.
39. Prusiner SB. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
40. Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. 1984. Purification and structural studies of a major scrapie prion protein. Cell 38:127-134.
41. Prusiner SB. 2004. Prion biology and diseases, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
42. Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K. 1997. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413:282-288.
43. Sajnani G, Pastrana MA, Dynin I, Onisko B, Requena JR. 2008. Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry. J. Mol. Biol. 382:88-98.
44. Sakudo A, et al. 2003. Absence of superoxide dismutase activity in a soluble cellular isoform of prion protein produced by baculovirus expression system. Biochem. Biophys. Res. Commun. 307:678-683.
45. Samson AO, Levitt M. 2011. Normal modes of prion proteins: from native to infectious particle. Biochemistry 50:2243-2248.
46. Scheibel T, Bloom J, Lindquist SL. 2004. The elongation of yeast prion fibers involves separable steps of association and conversion. Proc. Natl. Acad. Sci. U. S. A. 101:2287-2292.
47. Scott MR, Köhler R, Foster D, Prusiner SB. 1992. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1:986-997.
48. Solforosi L, et al. 2007. Toward molecular dissection of PrPC-PrPSc interactions. J. Biol. Chem. 282:7465-7471.
49. Stork M, Giese A, Kretzschmar HA, Tavan P. 2005. Molecular dynamics simulations indicate a possible role of parallel β-helices in seeded aggregation of poly-Gln. Biophys. J. 88:2442-2451.
50. Taraboulos A, Serban D, Prusiner SB. 1990. Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J. Cell Biol. 110:2117-2132.
51. Veith NM, Plattner H, Stuermer CA, Schulz-Schaeffer WJ, Bürkle A. 2009. Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy. Eur. J. Cell Biol. 88:45-63.
52. Wille H, et al. 2002. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. U. S. A. 99:3563-3568.
53. Williamson RA, et al. 1998. Mapping the prion protein using recombinant antibodies. J. Virol. 72:9413-9418.
54. Yamada M, et al. 1993. A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Sträussler-Scheinker disease. Neurology 43:2723-2724.