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Research Paper

Yeast-based screening of natural product extracts results in the identification of prion inhibitors from a marine sponge

ORCID Icon, ORCID Icon, ORCID Icon & ORCID Icon
Pages 234-244 | Received 26 Apr 2018, Accepted 07 Aug 2018, Published online: 13 Sep 2018

References

  • Prusiner SB. Prions. Proc Natl Acad Sci USA. 1998;95:13363–13383.
  • Prusiner SB. Molecular biology of prion diseases. Science. 1991;252:1515–1522.
  • Collinge J, Sidle KC, Meads J, et al. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature. 1996;383:685–690.
  • Seelig DM, Goodman PA, Skinner PJ. Potential approaches for heterologous prion protein treatment of prion diseases. Prion. 2016;10:18–24.
  • Scheckel C, Aguzzi A. Prions, prionoids and protein misfolding disorders. Nat Rev Genet. 2018;19:405–418.
  • Antony H, Wiegmans AP, Wei MQ, et al. Potential roles for prions and protein-only inheritance in cancer. Cancer Metastasis Rev. 2012;31:1–19.
  • Imberdis T, Heeres JT, Yueh H, et al. Identification of anti-prion compounds using a novel cellular assay. J Biol Chem. 2016;291:26164–26176.
  • Maplestone RA, Stone MJ, Williams DH. The evolutionary role of secondary metabolites – a review. Gene. 1992;115:151–157.
  • Newman DJ, Cragg GM. Natural products as sources of new drugs from 1981 to 2014. J Nat Prod. 2016;79:629–661.
  • Solassol J, Crozet C, Lehmann S. Prion propagation in cultured cells. Br Med Bull. 2003;66:87–97.
  • Wickner RB. [URE3] as an altered Ure2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 1994;264:566–569.
  • Bach S, Talarek N, Andrieu T, et al. Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol. 2003;21:1075–1081.
  • Tribouillard D, Bach S, Gug F, et al. Using budding yeast to screen for anti-prion drugs. ‎Biotechnol J. 2006;1:58–67.
  • Wickner RB, Masison DC, Edskes HK. [PSI+] and [URE3] as yeast prions. Yeast. 1995;11:1671–1685.
  • Smirnov M, Smirnov V, Budowsky E, et al. Red pigment of adenine-deficient yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1967;27:299–304.
  • Shewmaker F, Mull L, Nakayashiki T, et al. Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae. Genetics. 2007;176:1557–1565.
  • Liebman SW, Chernoff YO. Prions in yeast. Genetics. 2012;191:1041–1072.
  • Coschigano PW, Magasanik B. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol Cell Biol. 1991;11:822–832.
  • Bach S, Tribouillard D, Talarek N, et al. A yeast-based assay to isolate drugs active against mammalian prions. Methods. 2006;39:72–77.
  • Bruschi CV, Chuba PJ. Nonselective enrichment for yeast adenine mutants by flow cytometry. Cytometry. 1988;9:60–67.
  • Teasdale PR, Hayward S, Davison W. In situ, high-resolution measurement of dissolved sulfide using diffusive gradients in thin films with computer-imaging densitometry. Anal Chem. 1999;71:2186–2191.
  • Tribouillard-Tanvier D, Beringue V, Desban N, et al. Antihypertensive drug Guanabenz is active in vivo against both yeast and mammalian prions. PLoS One. 2008;3:e1981.
  • Feher M, Schmidt JM. Property distributions: differences between drugs, natural products, and molecules from combinatorial chemistry. J Chem Inf Comput Sci. 2003;43:218–227.
  • Xynas R, Capon R. Two new bromotyrosine-derived metabolites from an Australian marine sponge, Aplysina sp. Aust J Chem. 1989;42:1427–1433.
  • Kobayashi J, Honma K, Sasaki T, et al. Purealidins J-R, new bromotyrosine alkaloids from the Okinawan marine sponge Psammaplysilla purea. Chem Pharm Bull. 1995;43:403–407.
  • Hamann MT, Scheuer PJ, Kelly-Borges M. Biogenetically diverse, bioactive constituents of a sponge, order Verongida: bromotyramines and sesquiterpene-shikimate derived metabolites. J Org Chem. 1993;58:6565–6569.
  • Tsukamoto S, Kato H, Hirota H, et al. Ceratinamine: an unprecedented antifouling cyanoformamide from the marine sponge Pseudoceratina purpurea. J Org Chem. 1996;61:2936–2937.
  • Tilvi S, Rodrigues C, Naik CG, et al. New bromotyrosine alkaloids from the marine sponge Psammaplysilla purpurea. Tetrahedron. 2004;60:10207–10215.
  • Ishibashi M, Tsuda M, Ohizumi Y, et al. Purealidin A, a new cytotoxic bromotyrosine-derived alkaloid from the Okinawan marine sponge Psammaplysilla purea. Experientia. 1991;47:299–300.
  • Ortlepp S, Sjoegren M, Dahlstroem M, et al. Antifouling activity of bromotyrosine-derived sponge metabolites and synthetic analogues. Mar Biotechnol. 2007;9:776–785.
  • Gotsbacher MP, Karuso P. New antimicrobial bromotyrosine analogues from the sponge Pseudoceratina purpurea and its predator Tylodina corticalis. Mar Drugs. 2015;13:1389–1409.
  • Olatunji OJ, Ogundajo AL, Oladosu IA, et al. Non-competitive inhibition of acetylcholinesterase by bromotyrosine alkaloids. Nat Prod Commun. 2014;9:1559–1561.
  • Tian L-W, Feng Y, Shimizu Y, et al. Aplysinellamides A–C, bromotyrosine-derived metabolites from an Australian Aplysinella sp. Marine Sponge J Nat Prod. 2014;77:1210–1214.
  • Schoenfeld RC, Lumb J-P, Fantini J, et al. Total synthesis of mololipids: a new series of anti-HIV Moloka’iamine derivatives. Bioorg Med Chem Lett. 2000;10:2679–2681.
  • Brogan JT, Stoops SL, Crews BC, et al. Total synthesis of (+)-7-bromotrypargine and unnatural analogues: biological evaluation uncovers activity at CNS targets of therapeutic relevance. ACS Chem Neurosci. 2011;2:633–639.
  • Morisset S, Rouleau A, Ligneau X, et al. High constitutive activity of native H3 receptors regulates histamine neurons in brain. Nature. 2000;408:860–864.
  • Torrent J, Vilchez-Acosta A, Muñoz-Torrero D, et al. Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases. Acta Neuropathol Commun. 2015;3:18.
  • Doh-Ura K, Ishikawa K, Murakami-Kubo I, et al. Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models. J Virol. 2004;78:4999–5006.
  • Vishnevskaya AB, Kushnirov VV, Ter-Avanesyan MD. Neurodegenerative amyloidoses: yeast model. Mol Biol. 2007;41:308–315.
  • Prusiner SB, Woerman AL, Mordes DA, et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism. Proc Natl Acad Sci USA. 2015;112:E5308–E5317.

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