Prion rods contain an inert polysaccharide scaffold

Biological Chemistry

Volumn 380, Issue 11, 1999, Pages 1295-1306

  Appel, Thomas R ^a,c   Dumpitak, Christian ^a,c   Matthiesen, Uwe ^b   Riesner, Detlev ^a,c  

^a Institut für Angewandte Physik   (Germany)

^b Zentralinstitut Klin Chem L   (Germany)

^c HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Alditol acetates; Carbohydrate analysis; Methylation analysis; Prions; PrP; Scrapie

Indexed keywords

GLUCOSE; GLYCOSYLATED PROTEIN; POLYSACCHARIDE; PRION PROTEIN; PROTEINASE K;

ANIMAL TISSUE; ARTICLE; BRAIN; CARBOHYDRATE ANALYSIS; HAMSTER; HYDROLYSIS; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; SCRAPIE;

ANIMALIA; CRICETINAE;

EID: 0032758721     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.165     Document Type: Article

References (63)

1. Adams, D.H., and Caspary, E.A. (1967). Nature of the scrapie agent. Brit. Med. J. 2, 173.
2. Adams, D.H., and Field, E.J. (1968). The infective process in scrapie. Lancet 2, 714-716.
3. Adams, D.H., Field, E.J., and Joyce, G. (1972). Periodate - an inhibitor of the scrapie agent? Res. Vet. Sci. 13, 195-198.
4. Albersheim, P., Nevins, D.J., English, P.D., and Karr, A. (1967). A method for the analysis of sugars in plant cell-wall polysaccharides by gas-liquid chromatography. Carbohydr. Res. 5, 340-345.
5. Bessen, R.A., Kocisko, D.A., Raymond, G.J., Nandan, S., Lansbury, P.T., and Caughey, B. (1995). Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375, 698-700.
6. Biermann, C.J., and McGinnis, G.D., eds. (1989). Analysis of Carbohydrates by GLC and MS. (Boca Raton, Florida, USA: CRC-Press, Inc).
7. Blakeney, A.B., and Stone, B.A. (1985). Methylation of carbohydrates with lithium methylsulphinyl carbanion. Carbohydr. Res. 140, 319-324.
8. Blakeney, A.B., Harris, P.J., Henry, R.J., and Stone, B.A. (1983). A simple and rapid preparation of alditol acetates for monosaccharide analysis. Carbohydr. Res. 113, 291-299.
9. Blum, H., Beier, H., and Gross, H.H. (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
10. Brown, P., and Bradley, R. (1998). 1755 and all that: a historical primer of transmissible spongiform encephalopathy. Brit. Med. J. 317, 1688-1692.
11. Carlson, G.A. (1996). Prion strains. Curr. Top. Microbiol. Immunol. 207, 35-47.
12. Carp, R.I., Meeker, H., and Sersen, E. (1997). Scrapie strains retain their distinctive characteristics following passages of homogenates from different brain regions and spleen. J. Gen. Virol. 78, 283-290.
13. Carpita, N.C., and Shea, E.M. (1989). Linkage structure of carbohydrates by gas chromatography-mass spectrometry (GC-MS) of partially methylated alditol acetates. In: Analysis of Carbohydrates by GLC and MS, C.J. Biermann and G.D. McGinnes, eds. (Boca Raton, Florida, USA: CRC-Press, Inc.), pp. 157-216.
14. Caughey, B., Kocisko, D.A., Raymond, G.J., and Lansbury, P.T., Jr. (1995). Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2, 807-817.
15. Chambers, R.E., and Clamp, J.R. (1971). An assessment of methanolysis and other factors used in the analysis of carbohydrate-containing materials. Biochem. J. 125, 1009-1018.
16. Cruise, A.J., and Jefferey, J.W. (1959). Polysaccharide fibers in mammalian connective tissue. Nature 183, 677-678.
17. Diringer, H., Beekes, M., Özel, M., Simon, D., Queck, I., Cardone, F., Pocchiari, M., and Ironside, J.W. (1997). Highly infectious purified preparations of disease-specific amyloid of transmissible spongiform encephalopathies are not devoid of nucleic acids of viral size. Intervirology 40, 238-246.
18. Endo, T., Groth, D., Prusiner, S.B., and Kobata, A. (1989). Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28, 8380-8388.
19. Field, E.J. (1966). Transmission experiments with multiple sclerosis: an interim report. Brit. Med. J. 2, 564-565.
20. Field, E.J. (1967). The significance of astroglial hypertrophy in scrapie, kuru, multiple sclerosis and old age together with a note on the possible nature of the scrapie agent. Dt. Zeitschr. Nervenheilkunde 192, 265-274.
21. Goux, W.J., Rodriguez, S., and Sparkman, D.R. (1995). Analysis of the core components of Alzheimer paired helical filaments. A gas chromatography/mass spectrometry characterization of fatty acids, carbohydrates and long-chain bases. FEBS Lett. 366, 81-85.
22. Goux, W.J., Rodriguez, S., and Sparkman, D.R. (1996). Characterization of the glycolipid associated with Alzheimer paired helical filaments. J. Neurochem. 67, 723-733.
23. Hall, D.A., Lloyd, P.F., Saxl, H., and Happey, F. (1958). Mammalian cellulose. Nature 215, 1043-1044.
24. Hall, D.A., Happey, F., Lloyd, P.F., and Saxl, H. (1959). Oriented cellulose as a component of mammalian tissue. Proc. Royal Soc. Biol. 151, 497-516.
25. Hall, D.A., and Saxl, H. (1960). Human and other animal cellulose. Nature 187, 547-550.
26. Hall, D.A., and Saxl, H. (1961). Studies of human and tunicate cellulose and of their relation to reticulin. Proc. Royal Soc. Biol. 155, 202-217.
27. Hao, C., Ma, X., Fang, S., Liu, Z., Liu, S., Song, F., and Liu, J. (1998). Positive- and negative-ion matrix-assisted laser desorption/ionization mass spectrometry of saccharides. Rapid Comm. Mass Spectrom. 12, 345-348.
28. Harris, P.J., Henry, R.J., Blakeney, A.B., and Stone, B.A. (1984). An improved procedure for the methylation analysis of oligosaccharides and polysaccharides. Carbohydr. Res. 127, 59-73.
29. Hermentin, P. (1998). Kohlenhydratanalytik. In: Bioanalytik, F. Lottspeich, H. Zorbas, eds. (Heidelberg and Berlin, Germany: Spektrum Akademischer Verlag GmbH), p. 502.
30. Hill, A.F., Antoniou, M., and Collinge, J. (1999). Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80, 11-14.
31. Hounsell, E.F., Davies, M.J., and Smith, K.D. (1996). Determination of monosaccharide linkage and substitution patterns by GC-MS methylation analysis. In: The Protein Protocols Handbook, J.M. Walker, ed. (Totowa, NJ, USA: Humana Press, Inc.).
32. Hunter, G.D., Gibbons, R.A., Kimberlin, R.H., and Millson, G.C. (1969). Further studies of the infectivity and stability of extracts and homogenates derived from scrapie affected mouse brains. J. Comp. Pathol. 79, 101-108.
33. Jay, A. (1996). The methylation reaction in carbohydrate analysis. J. Carbohydr. Chem. 15, 897-923.
34. Kaneko, K., Peretz, D., Pan, K.M., Blochberger, T.C., Wille, H., Gabizon, R., Griffith, O.H., Cohen, F.E., Baldwin, M.A., and Prusiner, S.B. (1995). Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc. Natl. Acad. Sci. USA 91, 11160-11164.
35. Kascsak, R.J., Rubenstein, R., Merz, P.A., Tonna-DeMasi, M., Fersko, R., Carp, R.I., Wisniewski, H.M., and Diringer, H. (1987). Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61, 3688-3693.
36. Kellings, K., Meyer, N., Mirenda, C., Prusiner, S.B., and Riesner, D. (1992). Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. J. Gen. Virol. 73, 1025-1029.
37. 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.
38. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriaphage T4. Nature 227, 680-685.
39. McBride, P.A., Wilson, M.I., Eikelenboom, P., Tunstall, A., and Bruce, M.E. (1998). Heparan sulfate proteoglycan is associated with amyloid plaques and neuroanatomically targeted PrP pathology throughout the incubation period of scrapie-infected mice. Exp. Neurol. 149, 447-454.
40. McKinley, M.P., Braunfeld, M.B., Bellinger, C.G., and Prusiner, S.B. (1986). Molecular characteristics of prion rods purified from scrapie-infected hamster brain. J. Infect. Dis. 154, 110-120.
41. McKinley, M.P., Meyer, R.K., Kenaga, L., Rahbar, F., Cotter, R., Serban, A., and Prusiner, S.B. (1991). Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65, 1340-1351.
42. Parente, J.P., Cardon, P., Leroy, Y., Montreuil, J., Fournet, B, and Ricart, G. (1985). A convenient method for methylation of glycoprotein glycans in small amounts by using lithium methylsulfinyl carbanion. Carbohydr. Res. 141, 41-47.
43. Post, K., Pitschke, M., Schäfer, O., Wille, H., Appel, T.R., Kirsch, D., Mehlhorn, I., Serban, H., Prusiner, S.B., and Riesner, D. (1998). Rapid acquisition of β-sheet structure in the prion protein prior to multimer formation. Biol. Chem. 379, 1307-1317.
44. Prusiner, S.B. (1998). Prions. Proc. Natl. Acad. Sci. USA 95, 13363-13383.
45. Prusiner, S.B., Bolton, D.C., Groth, D.F., Bowman, K.A., Cochran, S.P., and McKinley, M.P. (1982). Further purification and characterization of scrapie prions. Biochemistry 21, 6942-6950.
46. Prusiner, S.B., McKinley, M.P., Bowman, K.A., Bolton, D.C., Bendheim, P.E., Groth, D.F., and Glenner, G.G. (1983). Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349-358.
47. Riesner, D., Kellings, K., Post, K., Wille, H., Serban, H., Groth, D., Baldwin, M.A., and Prusiner, S.B. (1996). Disruption of Prion rods generates 10-nm spherical particles having high α-helical content and lacking Scrapie infectivity. J. Virol. 70, 1714-1722.
48. Rudd, P.M., Endo, T., Colominas, C., Groth, D., Wheeler, S.F., Harvey, D.J., Wormald, M.R., Serban, H., Prusiner, S.B., Kobata, A., and Dwek, R.A. (1999). Glycosylation differences between the normal and the pathogenic prion isoforms. Proc. Natl. Acad. Sci. USA, in press.
49. Safar, J., Wang, W., Padgett, M.P., Ceroni, M., Piccardo, P., Zopf, D., Gajdusek, D.C., and Gibbs, C.J. (1990). Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer. Proc. Natl. Acad. Sci. USA 87, 6373-6377.
50. Safar, J., Wille, H., Itri, V., Groth, D., Serban, H., Torchia, M., Cohen, F.E., and Prusiner, S.B. (1998). Eight prion strains have PrP(Sc) molecules with different conformations. Nat. Med. 4, 1157-1165.
51. Selkoe, D.J., Ihara, Y., and Salazar, F.J. (1982). Alzheimer's disease: insolubility of partially purified paired helical filaments in sodium dodecyl sulfate and urea. Science 215, 1243-1245.
52. Singhrao, S.K., Morgan, B.P., Neal, J.W., and Newman, G.R. (1995). A functional role for Corpora amylacea based on evidence from complement studies. Neurodegeneration 4, 335-345.
53. Snow, A.D., Kisilevsky, R., Willmer, J., Prusiner, S.B., and DeArmond, S.J. (1989). Sulfated glycosaminoglycans in amyloid plaques of prion diseases. Acta Neuropathol. 77, 337-342.
54. Snow, A.D., Wight, T.N., Nochlin, D., Koike, Y., Kimata, K., DeArmond, S.J. and Prusiner, S.B. (1990). Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Sträussler syndrome, Creutzfeld-Jakob disease and scrapie. Lab. Invest. 63, 601-611.
55. Sparkman, D.R. (1993). X-ray probe microanalysis of Alzheimer disease soluble and insoluble paired helical filaments. Neurosci. Lett. 151, 153-157.
56. Stahl, N., Baldwin, M.A., Teplow, D., Hood, L., Beavis, R., Chait, B., Gibson, B.W., Burlingame, A.L., and Prusiner, S.B. (1992). Cataloguing post-translational modifications of the scrapie prion protein by mass spectroscopy. In: Prion diseases of humans and animals, S.B. Prusiner, J. Collinge, J. Powell, B. Anderton, eds. (Chichester, U.K.: Ellis Horwood, Ltd.).
57. Stahl, N., Baldwin, M.A., Teplow, D.B., Hood, L., Gibson, B.W., Burlingame, A.L., and Prusiner, S.B. (1993). Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002.
58. Stimson, E., Hope, J., Chong, A., and Burlingame, A.L. (1999). Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/ elecctrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38, 4855-4895.
59. Tagliavini, F., Prelli, F., Ghiso, J., Bugiani, O., Serban, D., Prusiner, S.B., Farlow, M.R., Ghetti, B., and Frangione, B. (1991). Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10, 513-519.
60. Tagliavini, F., Prelli, F., Porro, M., Rossi, G., Giaccone, G., Farlow, M.R., Dlouhy, S.R., Ghetti, B., Bugiani, O., and Frangione, B. (1994). Amyloid fibrils in Gerstmann-Sträussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele. Cell 79, 695-703.
61. Toriumi, J., Shirasawa, H., Sano, K., and Komatsu, K. (1972). Mammalian cellulose disease (watafuki disease) - a specific granulation tissue in conjunctiva producing cellulose. Acta Pathol. Japan 22, 591-612.
62. Wischik, C.M., Novak, M., Edwards, P.C., Klug, A., Tichelaar, W., and Crowther, R.A. (1988). Structural characterization of the core of the paired helical filament of Alzheimer disease. Proc. Natl. Acad. Sci. USA 85, 4884-4888.
63. Wisniewski, T., Aucouturier, P., Soto, C., and Frangione, B. (1998). The prionoses and other conformational disorders. Amyloid 5, 212-224.