Anti-prion activity of an RNA aptamer and its structural basis

Nucleic Acids Research

Volumn 41, Issue 2, 2013, Pages 1355-1362

  Mashima, Tsukasa ^a   Nishikawa, Fumiko ^b   Kamatari, Yuji O ^c   Fujiwara, Hiromichi ^a   Saimura, Masayuki ^a   Nagata, Takashi ^a   Kodaki, Tsutomu ^a   Nishikawa, Satoshi ^b   Kuwata, Kazuo ^c,d   Katahira, Masato ^a,d  

^a KYOTO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c GIFU UNIVERSITY   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; APTAMER; DIMER; MONOMER; PRION PROTEIN; RNA APTAMER; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANTIVIRAL ACTIVITY; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DRUG PROTEIN BINDING; DRUG STRUCTURE; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN SYNTHESIS INHIBITION; STRUCTURE ACTIVITY RELATION; TREATMENT OUTCOME;

ANIMALS; APTAMERS, NUCLEOTIDE; CATTLE; CELL LINE; MICE; MODELS, MOLECULAR; PEPTIDES; PRPC PROTEINS; PRPSC PROTEINS;

BOVINAE;

EID: 84875475933     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1132     Document Type: Article

References (30)

1. Prusiner, S.B. (1998) Prions. Proc. Natl Acad. Sci. USA, 95, 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. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA, 90, 10962-10966.
3. Prusiner, S.B., Scott, M.R., DeArmond, S.J. and Cohen, F.E. (1998) Prion protein biology. Cell, 93, 337-348. (Pubitemid 28232079)
4. Prusiner, S.B. (1982) Novel proteinaceous infectious particles cause scrapie. Science, 216, 136-144. (Pubitemid 12089840)
5. Prusiner, S.B. (1991) Molecular biology and transgenetics of prion diseases. Crit. Rev. Biochem. Mol. Biol., 26, 397-438. (Pubitemid 21892763)
6. Bueler, H., Aguzzi, A., Sailer, A., Greiner, R.A., Autenried, P., Aguet, M. and Weissmann, C. (1993) Mice devoid of PrP are resistant to scrapie. Cell, 73, 1339-1347. (Pubitemid 23201147)
7. Sailer, A., Bueler, H., Fischer, M., Aguzzi, A. and Weissmann, C. (1994) No propagation of prions in mice devoid of PrP. Cell, 77, 967-968. (Pubitemid 24208856)
8. Cashman, N.R. and Caughey, B. (2004) Prion diseases-close to effective therapy? Nat. Rev. Drug. Disc., 3, 874-884.
9. Mallucci, G. and Collinge, J. (2005) Rational targeting for prion therapeutics. Nat. Rev. Neurosci., 6, 23-34. (Pubitemid 40052136)
10. Sim, V.L. and Caughey, B. (2009) Recent advances in prion chemotherapeutics. Infect. Disord. Drug Targets, 9, 81-91.
11. Proske, D., Gilch, S., Wopfner, F., Schatzl, H.M., Winnacker, E.L. and Famulok, M. (2002) Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem, 3, 717-725. (Pubitemid 36004511)
12. Rhie, A., Kirby, L., Sayer, N., Wellesley, R., Disterer, P., Sylvester, I., Gill, A., Hope, J., James, W. and Tahiri-Alaoui, A. (2003) Characterization of 20-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J. Biol. Chem., 278, 39697-39705. (Pubitemid 37248531)
13. Vogtherr, M., Grimme, S., Elshorst, B., Jacobs, D.M., Fiebig, K., Griesinger, C. and Zahn, R. (2003) Antimalarial drug quinacrine binds to C-terminal helix of cellular prion protein. J. Med. Chem., 46, 3563-3564. (Pubitemid 36988643)
14. Kuwata, K., Nishida, N., Matsumoto, T., Kamatari, Y.O., Hosokawa-Muto, J., Kodama, K., Nakamura, H.K., Kimura, K., Kawasaki, M., Takakura, Y. et al. (2007) Hot spots in prion protein for pathogenic conversion. Proc. Natl Acad. Sci. USA, 104, 11921-11926. (Pubitemid 47185606)
15. Taubner, L.M., Bienkiewicz, E.A., Copie, V. and Caughey, B. (2010) Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. J. Mol. Biol., 395, 475-490.
16. Kimura, T., Hosokawa-Muto, J., Kamatari, Y.O. and Kuwata, K. (2011) Synthesis of GN8 derivatives and evaluation of their antiprion activity in TSE-infected cells. Bioorg. Med. Chem. Lett., 21, 1502-1507.
17. Schutz, A.K., Soragni, A., Hornemann, S., Aguzzi, A., Ernst, M., Bockmann, A. and Meier, B.H. (2011) The amyloid-Congo red interface at atomic resolution. Angew. Chem. Int. Ed. Engl., 50, 5956-5960.
18. Murakami, K., Nishikawa, F., Noda, K., Yokoyama, T. and Nishikawa, S. (2008) Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant prion protein and its b isoform with high affinity. Prion, 2, 73-78.
19. Nishikawa, F., Murakami, K., Matsugami, A., Katahira, M. and Nishikawa, S. (2009) Structural studies of an RNA aptamer containing GGA repeats under ionic conditions using microchip electrophoresis, circular dichroism, and 1D-NMR. Oligonucleotides, 19, 179-190.
20. Mashima, T., Matsugami, A., Nishikawa, F., Nishikawa, S. and Katahira, M. (2009) Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein. Nucleic Acids Res., 37, 6249-6258.
21. Garc, F.L., Zahn, R., Riek, R. and Wuthrich, K. (2000) NMR structure of the bovine prion protein. Proc. Natl Acad. Sci. USA, 97, 8334-8339. (Pubitemid 30639673)
22. Nishida, N., Harris, D.A., Vilette, D., Laude, H., Frobert, Y., Grassi, J., Casanova, D., Milhavet, O. and Lehmann, S. (2000) Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J. Virol., 74, 320-325. (Pubitemid 30002912)
23. Brunger, A.T. (1993) X-PLOR Version 3.1: A System for X-ray Crystallography and NMR. New Haven, Yale University Press.
24. Schwieters, C.D., Kuszewski, J.J., Tjandra, N. and Clore, G.M. (2003) The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson., 160, 65-73.
25. Furukawa, A., Nagata, T., Matsugami, A., Habu, Y., Sugiyama, R., Hayashi, F., Kobayashi, N., Yokoyama, S., Takaku, H. and Katahira, M. (2009) Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. EMBO J., 28, 440-451.
26. Wuthrich, K. (1986) NMR of Protein and Nucleic Acids. John Wiley & Sons, New York, NY.
27. Campisi, D.M., Calabro, V. and Frankel, A.D. (2001) Structure-based design of a dimeric RNA-peptide complex. EMBO J., 20, 178-186. (Pubitemid 32099114)
28. Hara, H., Okemoto-Nakamura, Y., Shinkai-Ouchi, F., Hanada, K., Yamakawa, Y. and Hagiwara, K. (2012) Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrPC to PrPSc in prion-infected neuroblastoma cells. J. Virol., 86, 5626-5636.
29. Matsugami, A., Ouhashi, K., Kanagawa, M., Liu, H., Kanagawa, S., Uesugi, S. and Katahira, M. (2001) An intramolecular quadruplex of (GGA)4 triplet repeat DNA with a G:G:G:G tetrad and a G(:A):G(:A):G(:A):G heptad, and its dimeric interaction. J. Mol. Biol., 313, 255-269. (Pubitemid 33587186)
30. Lauren, J., Gimbel, D.A., Nygaard, H.B., Gilbert, J.W. and Strittmatter, S.M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-b oligomers. Nature, 457, 1128-1132.