Effects of new amphotericin analogues on the scrapie isoform of the prion protein

Biochimica et Biophysica Acta - General Subjects

Volumn 1780, Issue 10, 2008, Pages 1162-1167

  Soler, Lara ^a   Caffrey, Patrick ^a   McMahon, Hilary E M ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Amphotericin; Analogues; Prion; Scrapie

Indexed keywords

16 DESCARBOXYL 16 METHYL 19 O (6 DEOXYHEXOSYL) 19 O DESMYCOSAMINYLAMPHOTERICIN; 16 DESCARBOXYL 16 METHYLAMPHOTERICIN B; 3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; AMPHOTERICIN B; CARBOXYL GROUP; ISOPROTEIN; METHYL GROUP; PRION PROTEIN;

ANIMAL CELL; ARTICLE; CANCER CELL CULTURE; CELL CULTURE; CONTROLLED STUDY; CULTURE MEDIUM; DRUG CYTOTOXICITY; DRUG EFFECT; DRUG STRUCTURE; IC 50; NEUROBLASTOMA CELL; NITROBLUE TETRAZOLIUM TEST; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; RAT; STRUCTURE ANALYSIS;

AMPHOTERICIN B; ANIMALS; ANTIOXIDANTS; ASCORBIC ACID; CATALASE; CELL LINE, TUMOR; CELL SURVIVAL; INHIBITORY CONCENTRATION 50; MICE; POLYENES; PROTEIN ISOFORMS; PRPSC PROTEINS;

EID: 50949110043     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.07.005     Document Type: Article

References (32)

1. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13363-13383
2. Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F.E., et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 10962-10966
3. Safar J., Roller P.P., Gajdusek D.C., and Gibbs Jr. C.J. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268 (1993) 20276-20284
4. Meyer R.K., McKinley M.P., Bowman K.A., Braunfeld M.B., Barry R.A., and Prusiner S.B. Separation and properties of cellular and scrapie prion proteins. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 2310-2314
5. Weissmann C. The state of the prion. Nat. Rev. Microbiol. 2 (2004) 861-871
6. Wong C., Xiong L.W., Horiuchi M., Raymond L., Wehrly K., Chesebro B., and Caughey B. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. Embo. J. 20 (2001) 377-386
7. Adler V., Zeiler B., Kryukov V., Kascsak R., Rubenstein R., and Grossman A. Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro. J. Mol. Biol. 332 (2003) 47-57
8. Leucht C., Simoneau S., Rey C., Vana K., Rieger R., Lasmezas C.I., and Weiss S. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO. Rep. 4 (2003) 290-295
9. Ludewigs H., Zuber C., Vana K., Nikles D., Zerr I., and Weiss S. Therapeutic approaches for prion disorders. Expert. Rev. Anti. Infect. Ther. 5 (2007) 613-630
10. Stewart L.A., Rydzewska L.H., Keogh G.F., and Knight R.S. Systematic review of therapeutic interventions in human prion disease. Neurology 70 (2008) 1272-1281
11. Ladogana A., Casaccia P., Ingrosso L., Cibati M., Salvatore M., Xi Y.G., Masullo C., and Pocchiari M. Sulphate polyanions prolong the incubation period of scrapie-infected hamsters. J. Gen. Virol. 73 Pt 3 (1992) 661-665
12. Ingrosso L., Ladogana A., and Pocchiari M. Congo red prolongs the incubation period in scrapie-infected hamsters. J. Virol. 69 (1995) 506-508
13. Demaimay R., Adjou K.T., Beringue V., Demart S., Lasmezas C.I., Deslys J.P., Seman M., and Dormont D. Late treatment with polyene antibiotics can prolong the survival time of scrapie-infected animals. J. Virol. 71 (1997) 9685-9689
14. Adjou K.T., Demaimay R., Deslys J.P., Lasmezas C.I., Beringue V., Demart S., Lamoury F., Seman M., and Dormont D. MS-8209, a water-soluble amphotericin B derivative, affects both scrapie agent replication and PrPres accumulation in Syrian hamster scrapie. J. Gen. Virol. 80 Pt 4 (1999) 1079-1085
15. Gupta A.K., and Tomas E. New antifungal agents. Dermatol. Clin. 21 (2003) 565-576
16. Goldman R.D., Ong M., Wolpin J., Doyle J., Parshuram C., and Koren G. Pharmacological risk factors for amphotericin B nephrotoxicity in children. J. Clin. Pharmacol. 47 (2007) 1049-1054
17. Baginski M., Czub J., and Sternal K. Interaction of amphotericin B and its selected derivatives with membranes: molecular modeling studies. Chem. Rec. 6 (2006) 320-332
18. Baginski M., Resat H., and Borowski E. Comparative molecular dynamics simulations of amphotericin B-cholesterol/ergosterol membrane channels. Biochim. Biophys. Acta. 1567 (2002) 63-78
19. Mange A., Nishida N., Milhavet O., McMahon H.E., Casanova D., and Lehmann S. Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures. J. Virol. 74 (2000) 3135-3140
20. Carmody M., Murphy B., Byrne B., Power P., Rai D., Rawlings B., and Caffrey P. Biosynthesis of amphotericin derivatives lacking exocyclic carboxyl groups. J. Biol. Chem. 280 (2005) 34420-34426
21. Byrne B., Carmody M., Gibson E., Rawlings B., and Caffrey P. Biosynthesis of deoxyamphotericins and deoxyamphoteronolides by engineered strains of Streptomyces nodosus. Chem. Biol. 10 (2003) 1215-1224
22. Li R., Liu T., Wong B.S., Pan T., Morillas M., Swietnicki W., O'Rourke K., Gambetti P., Surewicz W.K., and Sy M.S. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301 (2000) 567-573
23. Prior M., Lehmann S., Sy M.S., Molloy B., and McMahon H.E. Cyclodextrins inhibit replication of scrapie prion protein in cell culture. J. Virol. 81 (2007) 11195-11207
24. Brajtburg J., Elberg S., Schwartz D.R., Vertut-Croquin A., Schlessinger D., Kobayashi G.S., and Medoff G. Involvement of oxidative damage in erythrocyte lysis induced by amphotericin B. Antimicrob. Agents. Chemother. 27 (1985) 172-176
25. Poljsak B., and Raspor P. The antioxidant and pro-oxidant activity of vitamin C and trolox in vitro: a comparative study. J. Appl. Toxicol. (2007)
26. Demaimay R., Harper J., Gordon H., Weaver D., Chesebro B., and Caughey B. Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation. J. Neurochem. 71 (1998) 2534-2541
27. Milhavet O., McMahon H.E., Rachidi W., Nishida N., Katamine S., Mange A., Arlotto M., Casanova D., Riondel J., Favier A., and Lehmann S. Prion infection impairs the cellular response to oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 13937-13942
28. Requena J.R., Groth D., Legname G., Stadtman E.R., Prusiner S.B., and Levine R.L. Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7170-7175
29. Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., and Prusiner S.B. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell. Biol. 129 (1995) 121-132
30. Bate C., Salmona M., Diomede L., and Williams A. Squalestatin cures prion-infected neurons and protects against prion neurotoxicity. J. Biol. Chem. 279 (2004) 14983-14990
31. Adjou K.T., Demaimay R., Lasmezas C.I., Seman M., Deslys J.P., and Dormont D. Differential effects of a new amphotericin B derivative, MS-8209, on mouse BSE and scrapie: implications for the mechanism of action of polyene antibiotics. Res. Virol. 147 (1996) 213-218
32. Cheron M., Cybulska B., Mazerski J., Grzybowska J., Czerwinski A., and Borowski E. Quantitative structure-activity relationships in amphotericin B derivatives. Biochem. Pharmacol. 37 (1988) 827-836