Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution

Archives of Virology

Volumn 143, Issue 7, 1998, Pages 1251-1263

  Nandi, P K ^a  

^a CEMAGREF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CONFORMATIONAL TRANSITION; DNA CONFORMATION; FLUORESCENCE; HUMAN PRION PEPTIDE; PH; POLYMER; POLYMERIZATION; THIOFLAVINE;

AMINO ACID SEQUENCE; AMYLOID; ANILINO NAPHTHALENESULFONATES; ANIMALS; DNA; FLUORESCENT DYES; HUMANS; HYDROGEN-ION CONCENTRATION; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; POLYMERS; PRION DISEASES; PRIONS; PROTEIN BINDING; SOLUTIONS; THIAZOLES;

SCRAPIE PRION;

EID: 0031875169     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007050050373     Document Type: Article

References (57)

1. Prusiner SB (1996) Molecular biology and pathogenesis of prion diseases. Trends Biochem Sci 21: 482-487
2. Prusiner SB (1994) Biology and genetics of prion diseases Annu Rev Microbiol 48: 655-686
3. Baldwin MA, Cohen FE, Prusiner SB (1995) Prion protein isoforms, a convergence of biological and structural investigations. J Biol Chem 270: 19 197-19200
4. Weissmann C (1996) Molecular biology of transmissible spongiform encephalopathies. FEBS Lett 389: 3-11
5. Weissman C (1995) Yielding under strain. Nature 375: 628-629
6. Caughey B, Chesbro B (1997) Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol 7: 56-62
7. Griffith JS (1967) Self replication and scrapie. Nature 215: 1043-1044
8. Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30: 7672-758
9. Pan K-M, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Melhorn I, Huang Z, Fletterick RJ, Cohen FE, Prusiner SB (1993) Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962-10966
10. Telling GC, Parchi P. DeArmond SJ, Cortelli P, Montagna P, Gabizon R, Mastrianni J, Lugaresi E, Gambetti P, Prusiner SB (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274: 2079-2082
11. Özel M, Diringer H (1994) Small virus-like structure in fractions from scrapie hamster brain. Lancet 343: 894-895
12. Diringer H, Beeks M, Oberdieck U (1994) The nature of the scrapie agent: the virus theory. Ann NY Acad Sci 724: 246-258
13. Sklaviadis T, Akowitz E, Manuelidis E, Manuelodis L (1993) Nucleic acid binding proteins in highly purified Creutzfeldt-Jakob disease preparations. Proc Natl Acad Sci USA 90: 5 713-5 717
14. Manuelidis L, Fritch W (1996) Infectivity and host response in Creutzfeldt-Jakob disease. Virology 216: 46-59
15. Grady D (1996) Ironing out the wrinkles in the prion strain problem. Science 274: 2010
16. Pochiari M (1994) Prion and related neurological diseases. Mol Aspects Med 15: 195-291
17. Lesmézas CI, Deslys JP, Robain O, Jaegly A, Beringue V, Peyrin J-M, Fournier J-G, Hauw J-J, Rossier J, Dormont D (1997) Transmission of the BSE-agent to mice in the absence of detectable abnormal prion protein. Science 275: 402-425
18. Hunter N, Cairns D, Foster JD, Smith G, Goldmann W, Donnelly K (1997) Is scrapie solely a genetic disease? Nature 386: 137
19. Chesbro B (1997) Human TSE disease - viral or protein only? Nature Med 3: 491-492
20. Silvestrini MC, Cardone F, Mars B, Pucci P, Barra D, Brunori M, Pocchiari M (1997) Identification of the prion protein allotypes which accumulate in the brain of sporadic and familial Creutzfeldt-Jakob disease patients. Nature Med 3: 521-525
21. Manuelidis L, Fritch W, Xi Y-G (1997) Evaluation of a strain of CJD that induces BSE-like plaques. Science 277: 94-98
22. Weissmann C (1991) A "unified theory" of prion propagation. Nature 352: 679-683
23. Bruce ME, Will RG, Ironside JW, McConnell I, Drummond D, Suttie A, McCardale L. Chree A, Hope J, Birkett C, Cousens S, Fraser H, Bostock CJ (1997) Transmission to mice indicate that "new variant" CJD is caused by the BSE agent. Nature 389: 498-501
24. 23a. Almond J, Pattison J (1997) Human BSE. Nature 389: 437-438
25. Tagliavini F, Prelli F, Verga L, Giaccone G, Sarma R, Gorevic P, Ghetti B, Passerini F, Ghibaudi E, Forloni G, Salmona M, Bigiani O, Frangione B (1993) Synthetic peptide homologous to prion protein residues 106-147 form amyloid in vitro. Proc Natl Acad Sci USA 90: 9 673-9 682
26. Goldfrab LG. Brown P, Haltia M, Ghiso J, Frangione B, Gajdusek C (1993) Synthetic peptides corresponding to different mutated regions of the amyloid gene in familial Creutzfeldt-Jakob disease show enhanced in vitro formation of morphologically different amyloid fibrils. Proc Natl Acad Sci USA 90: 4451-4454
27. Come JH, Fraser PE, Lansbury Jr PT (1993) A kinetic model for amyloid formation in the prion diseases: Importance of seeding. Proc Natl Acad Sci USA 90: 5 959-5 963
28. Gasset M, Baldwin MA, Lloyd DH, Gabriel JM, Holtzman DM, Cohen F, Fletterick R, Prusiner SB (1992) Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid. Proc Natl Acad Sci USA 89: 10 940-10 944
29. Gasset M, Baldwin MA, Fletteric RJ, Prusiner SB (1993) Perturbation of the secondary structure of the scrapie prion protein under conditions associated with changes in infectivity. Proc Natl Acad Sci USA 90: 1-5
30. Nguyen JT, Baldwin MA, Cohen FE, Prusiner SB (1995) Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry 34: 4 186-4 192
31. Zhang H, Kiyotoshi K, Nguyen JT, Livshits TL, Baldwin MA, Cohen FE, James TL, Prusiner SB (1995) Conformational transitions in peptides containing two putative α-helices of the prion protein. J Mol Biol 250: 514-526
32. Selvaggini C, De Gioia L, Cantu L, Ghibaudi E, Diomede L, Passerini F, Forloni G, Bugiani O, Tagliavini F, Salmona M (1993) Molecular characteristics of a protease resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem Biophys Res Commun 194: 1 380-1 385
33. De Gioia L, Selvaggini C, Ghibaudi G, Diomede L, Bugiani O, Forloni G, Tagliavini F, Salmona M (1994) Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J Biol Chem 269: 7 859-7 862
34. Forloni G, Angeretti N, Chiesa R, Monzani E, Salmona M, Bugiani O, Tagliavini F (1993) Neurotoxicity of a prion protein fragment. Nature 362: 543-546
35. Brown DR, Schmidt B, Kretzschmar HA (1996) Role of microgilia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380: 345-347
36. Chen SG, Teplow DB, Parehi P, Teller JK, Gambetti P, Autilio-Gambetti L (1995) Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem 270: 19 173-19 180
37. Doh-ura K, Tateishi J, Sasaki H, Kitamoto T, Sakai Y (1989) Pro to leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndrome. Biochem Biophys Res Commun, 163: 974-979
38. Han H, Weinerb PH, Lansbury Jr, PT (1995) The core Alzheimer's peptide NAC forms amyloid firbils which seed and are seeded by β-amyloid: is NAC a common trigger or target in neurodegenerative disease? Chem Biol 2: 163-169
39. Safar J, Roller PP, Gajdusek, DC, Gibbs Jr, CJ (1994) Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33: 8 375-8 383
40. Öesch B, Westaway D, Walchli M, Mckinley MP, Kent SBH, Aebersold R, Barry RA, Tempst P, Teplow DB, Hood LE, Prusiner SB, Weissmann C (1985) A cellular gene encodes scrapie PrP 27-30 protein. Cell 40: 735-746
41. Horneman S, Korth C, Öesch B, Riek R, Wider G, Wuthrich K, Glockshuber R (1997) Recombinant full-length murine prion protein, mPrP (23-231); purification and spectroscopic characterization. FEBS Lett 413: 277-281
42. 40a. Riek R, Horneman S, Wider G, Glockshuber R, Wuthrich K (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231). FEBS Lett 413: 282-288
43. Zhang H, Stockel J, Mehlhorn I, Groth D, Baldwin MA, Prusiner SB, James TL, Cohen FE (1997) Physical studies of conformational plasticity in a recombinant prion protein. Biochemistry 36: 3 543-3 553
44. Nandi PK (1997) The properties of prion peptide amyloid in solution. Eur Biophys J 26: 29
45. Nandi PK (1997) Interaction of prion peptide HuPrp 106-126 with nucleic acid. Arch Virol 142: 2 537-2 545
46. Schaper S, Messer W (1997) Prediction of the structure of the replication initiator protein DnaA. Proteins 28: 1-9
47. Bolens R, Vis H, Vorgias CE, Wilson KS, Kaptein R (1996) Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy. Biopolymers 40: 553-559
48. Konrat R, Weiskirchen R, Krautler B, Bister K (1997) Solution structure of the carboxyterminal LIM domain from quail cysteine-rich protein CRP2. J Biol Chem 272: 12 001-12 007
49. Church GM, Sussman JL, Kim SH (1997) Secondary structural complimentarity between DNA and protein. Proc Natl Acad Sci USA 74: 1 458-1 462
50. LeVine III H, (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2: 404-410
51. Wood SJ, Maleef B, Hart T, Wetzel R (1996) Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J Mol Biol 256: 870-877
52. Bloomfield VA (1991) Codensation of DNA by multivalent cations: consideration of the mechanism. Biopolymers 31: 1 471-1 481
53. Oosawa F, Kasai M (1962) A theory of linear and helical aggregation of macromolecules. J Mol Biol 4: 10-21
54. Cantor C, Schimmel R (1980) Biophysical Chemistry Part 1. WH Freeman, San Francisco, pp 145-150
55. Dickinson AG, Outram GW (1998) Genetic aspects of unconventional virus infections: the basis of the virino hypothesis. Ciba Found Symp 135: 63-83
56. Soto C, Castano EM, Frangione B, Inestrosa NC (1995) The α-helical to β-strand transition in the amino-terminal fragment of the amyloid-peptide modulates amyloid formation. J Biol Chem 270: 3 063-3 067
57. Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D (1992) Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J Gen Virol 73: 1 025-1 029