Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells

Journal of General Virology

Volumn 81, Issue 4, 2000, Pages 1155-1164

  Rudyk, Hélène ^a   Vasiljevic, Snezana ^b   Hennion, Ruth M ^b   Birkett, Christopher R ^b   Hope, James ^b   Gilbert, Ian H ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

^b INSTITUTE FOR ANIMAL HEALTH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CONGO RED; PRION PROTEIN;

ARTICLE; PRIORITY JOURNAL; SCRAPIE AGENT; STRUCTURE ACTIVITY RELATION;

OVIS ARIES; SCRAPIE PRION;

EID: 0034109546     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-81-4-1155     Document Type: Article

References (57)

1. Anderson, R. M., Donnelly, C. A., Ferguson, N. M., Woolhouse, M. E. J., Watt, C. J., Udy, H. J., MaWhinney, S., Dunstan, S. P., Southwood, T. R. E., Wilesmith, J. W., Ryan, J. B. M., Hoinville, L. J., Hillerton, J. E., Austin, A. R. & Wells, G. A. H. (1996). Transmission dynamics and epidemiology of BSE in British cattle. Nature 382, 779-788.
2. Bandiera, T., Lansen, J., Post, C. & Varasi, M. (1997). Inhibitors of Aβ peptide aggregation as potential anti-Alzheimer agents. Current Medicinal Chemistry 4, 159-170.
3. Basler, K., Oesch, B., Scott, M., Westaway, D., Walchli, M., Groth, D. F., McKinley, M. P., Prusiner, S. B. & Weissmann, C. (1986). Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46, 417-428.
4. Beck, E., Daniel, P. M., Davey, A. J., Gajdusek, D. C. & Gibbs, C. J., Jr (1982). The pathogenesis of transmissible spongiform encephalopathy: an ultrastructural study. Brain 105, 755-786.
5. Beekes, M., McBride, P. A. & Baldauf, E. (1998). Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie. Journal of General Virology 79, 601-607.
6. Bolton, D. C., Meyer, R. K. & Prusiner, S. B. (1985). Scrapie PrP 27-30 is a sialoglycoprotein. Journal of Virology 53, 596-606.
7. Bos, R. P., Koopman, J. P., Theuws, J. L. G. & Henderson, P. T. (1987). The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: internal exposure of rats to benzidine after intestinal azo reduction. Mutation Research 181, 327.
8. Brinkworth, R. I. & Fairlie, D. P. (1992). Non-peptidic anti-AIDS agents: inhibition of HIV-1 proteinase by disulfonates. Biochemical and Biophysical Research Communications 188, 624-630.
9. Bruce, M. E. & Fraser, H. (1975). Amyloid plaques in the brains of mice infected with scrapie: morphological variation and staining properties. Neuropathology and Applied Neurobiology 1, 189-202.
10. Bruce, M. E., Will, R. G., Ironside, J. W., McConnell, I., Drummond, D., Suttie, A., McCardle, L., Chree, A., Hope, J., Birkett, C., Cousens, S., Fraser, H. & Bostock, C. J. (1997). Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 389, 498-501.
11. Caspi, S., Halimi, M., Yanai, A., Ben Sasson, S., Taraboulos, A. & Gabizon, R. (1998). The anti-prion activity of Congo red. Putative mechanism. Journal of Biological Chemistry 273, 3484-3489.
12. Caughey, B. (1994). Scrapie-associated PrP accumulation and agent replication: effects of sulphated glycosaminoglycan analogues. Philosophical Transactions of the Royal Society of London Series B Biological Sciences 343, 399-404.
13. Caughey, B. & Raymond, G. J. (1993). Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. Journal of Virology 67, 643-650.
14. Caughey, B., Brown, K., Raymond, G. J., Katzenstein, G. E. & Thresher, W. (1994). Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red. Journal of Virology 68, 2135-2141.
15. Clarke, M. (1979). Infection of cell cultures with the scrapie agent. In Slow Transmissible Diseases of the Nervous System, pp. 225-233. Edited by S. Prusiner & W. Hadlow. New York: Academic Press.
16. Clarke, M. C. & Haig, D. A. (1970). Evidence for the multiplication of scrapie agent in cell culture. Nature 225, 100-101.
17. Demaimay, R., Harper, J., Gordon, H., Weaver, D., Chesebro, B. & Caughey, B. (1998). Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation. Journal of Neurochemistry 71, 2534-2541.
18. Edwards, R. A. & Woody, R. W. (1979). Spectroscopic studies of Cibacron Blue and Congo Red bound to dehydrogenases and kinases. Evaluation of dyes as probes of the dinucleotide fold. Biochemistry 18, 5197-5204.
19. Ehlers, B. & Diringer, H. (1984). Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. Journal of General Virology 65, 1325-1330.
20. Farquhar, C., Dickinson, A. & Bruce, M. (1999). Prophylactic potential of pentosan polysulphate in transmissible spongiform encephalopathies. Lancet 353, 117.
21. Gilbert, I. & Rudyk, H. (1999). Inhibitors of protease-resistant prion formation. International Antiviral News 7, 78-82.
22. Gray, L. E., Jr & Ostby, J. S. (1993). The effects of prenatal administration of azo dyes on testicular development in the mouse: a structure activity profile of dyes derived from benzidine, dimethylbenzidine, or dimethoxybenzidine. Fundamental and Applied Toxicology 20, 177-183.
23. Gray, L. E., Jr, Kavlock, R. J., Ostby, J. & Ferrell, J. (1983). The eratogenic effects of Congo red on the reproductive system of the male mouse. Teratology 27. A46.
24. Gray, L. E., Jr, Ostby, J. S., Kavlock, R. J. & Marshall, R. (1992). Gonadal effects of fetal exposure to the azo dye congo red in mice: infertility in female but not male offspring. Fundamental and Applied Toxicology 19, 411-422.
25. Hill, A. F., Butterworth, R. J., Joiner, S., Jackson, G., Rossor, M. N., Thomas, D. J., Frosh, A., Tolley, N., Bell, J. E., Spencer, M., King, A., Al-Sarraj, S., Ironside, J. W., Lantos, P. L. & Collinge, J. (1999). Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet 353, 183-189.
26. Hope, J., Morton, L. J. D., Farquhar, C. F., Multhaup, G., Beyreuther, K. & Kimberlin, R. H. (1986). The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO Journal 5, 2591-2597.
27. Hope, J., Multhaup, G., Reekie, L. J., Kimberlin, R. H. & Beyreuther, K. (1988). Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie. European Journal of Biochemistry 172, 271-277.
28. Ingrosso, L., Ladogana, A. & Pocchiari, M. (1995). Congo red prolongs the incubation period in scrapie-infected hamsters. Journal of Virology 69, 506-508.
29. Klunk, W. E., Debnath, M. L. & Pettegrew, J. W. (1994). Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease. Neurobiology of Aging 15, 691-698.
30. Ladogana, A., Casaccia, P., Ingrosso, L., Cibati, M., Salvatore, M., Xi, Y.-g., Masullo, C. & Pocchiari, M. (1992). Sulphate polyanions prolong the incubation period of scrapie-infected hamsters. Journal of General Virology 73, 661-665.
31. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
32. Liao, L. L., Horwitz, S. B., Huang, M. T., Grollman, A. P., Steward, D. & Martin, J. (1975). Triphenylmethane dyes as inhibitors of reverse transcriptase, ribonucleic acid polymerase, and protein synthesis. Journal of Medicinal Chemistry 18, 117-120.
33. McBride, P. A. & Beekes, M. (1999). Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie. Neuroscience Letters 265, 135-138.
34. McBride, P. A., Bruce, M. E. & Fraser, H. (1988). Immunostaining of scrapie cerebral amyloid plaques with antisera raised to scrapie-associated fibrils (SAF). Neuropathology and Applied Neurobiology 14, 325-336.
35. Masullo, C., Macchi, G., Xi, Y. G. & Pocchiari, M. (1992). Failure to ameliorate Creutzfeldt-Jakob disease with amphotericin B therapy. Journal of Infectious Diseases 165, 784-785.
36. Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A. & Prusiner, S. B. (1986). Separation and properties of cellular and scrapie prion proteins. Proceedings of the National Academy of Sciences, USA 83, 2310-2314.
37. Piekarska, B., Skowronek, M., Rybarska, J., Stopa, B., Roterman, I. & Konieczny, L. (1996). Congo red-stabilized intermediates in the lambda light chain transition from native to molten state. Biochimie 78, 183-189.
38. Pollack, S. J., Sadler, I. I. J., Hawtin, S. R., Tailor, V. J. & Shearman, M. S. (1995a). Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of beta-amyloid in rat PC12 cells. Neuroscience Letters 184, 113-116.
39. Pollack, S. J., Sadler, I. I. J., Hawtin, S. R., Tailor, V. J. & Shearman, M. S. (1995b). Sulfonated dyes attenuate the toxic effects of beta-amyloid in a structure-specific fashion. Neuroscience Letters 197, 211-214.
40. Priola, S. A., Caughey, B., Raymond, G. J. & Chesebro, B. (1994). Prion protein and the scrapie agent: in vitro studies in infected neuroblastoma cells. Infectious Agents and Disease 3, 54-58.
41. Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D. F. & Glenner, G. G. (1983). Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349-358.
42. Race, R. E., Fadness, L. H. & Chesebro, B. (1987). Characterization of scrapie infection in mouse neuroblastoma cells. Journal of General Virology 68, 1391-1399.
43. Rubenstein, R., Carp, R. I. & Callahan, S. M. (1984). In vitro replication of scrapie agent in a neuronal model: infection of PC12 cells. Journal of General Virology 65, 2191-2198.
44. Safar, J., Roller, P. P., Gajdusek, D. C. & Gibbs, C. J., Jr (1994). Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33, 8375-8383.
45. Shearman, M. S., Ragan, C. I. & Iversen, L. L. (1994). Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death. Proceedings of the National Academy of Sciences, USA 91, 1470-1474.
46. Skowronek, M., Stopa, B., Konieczny, L., Rybarska, J., Piekarska, B., Szneler, E., Bakalarski, G. & Roterman, I. (1998). Self-assembly of Congo Red - a theoretical and experimental approach to identify its supramolecular organization in water and salt solutions. Biopolymers 46, 267-281.
47. Stimson, E., Hope, J., Chong, A. & Burlingame, A. L. (1999). Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38, 4885-4895.
48. Stopa, B., Gorny, M., Konieczny, L., Piekarska, B., Rybarska, J., Skowronek, M. & Roterman, I. (1998). Supramolecular ligands: monomer structure and protein ligation capability. Biochimie 80, 963-968.
49. Taraboulos, A., Serban, D. & Prusiner, S. B. (1990). Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. Journal of Cell Biology 110, 2117-2132.
50. Tatzelt, J., Prusiner, S. B. & Welch, W. J. (1996). Chemical chaperones interfere with the formation of scrapie prion protein. EMBO Journal 15, 6363-6373.
51. Towbin, H. T., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences, USA 76, 4350-4354.
52. Turnell, W. G. & Finch, J. T. (1992). Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. Journal of Molecular Biology 227, 1205-1223.
53. Wells, G. A. H., Scott, A. C., Johnson, C. T., Gunning, R. F., Hancock, R. D., Jeffrey, M., Dawson, M. & Bradley, R. (1987). A novel progressive spongiform encephalopathy in cattle. Veterinary Record 121, 419-420.
54. Will, R. G., Ironside, J. W., Zeidler, M., Cousens, S. N., Estibeiro, K., Alperovitch, A., Poser, S., Pocchiari, M., Hofman, A. & Smith, P. G. (1996). A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925.
55. Wille, H., Baldwin, M. A., Cohen, F. E., DeArmond, S. J. & Prusiner, S. B. (1996). Prion protein amyloid: separation of scrapie infectivity from PrP polymers. Ciba Foundation Symposia 199, 181-199.
56. Zenser, T. V., Lakshmi, V. M. & Davis, B. B. (1998). N-glucuronidation of benzidine and its metabolites. Role in bladder cancer. Drug Metabolism and Disposition 26, 856-859.
57. Zollinger, H. (1987). Color Chemistry: Syntheses, Properties and Applications of Organic Dyes and Pigments. Weinheim: VCH.