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References

  1. Prusiner SB. 1998. Prions. Proc. Natl. Acad. Sci. USA 95:13363-13383.
    Pubmed CrossRef
  2. Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim P E, G roth D F, et al. 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
    CrossRef
  3. Aguzzi A, Lakkaraju AKK, Frontzek K. 2018. Toward therapy of human prion diseases. Annu. Rev. Pharmacol. Toxicol. 58: 331-351.
    Pubmed CrossRef
  4. Solassol J, Crozet C, Perrier V, Leclaire J, Beranger F, Caminade A-M, et al. 2004. Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie. J. Gen. Virol. 85: 1791-1799.
    Pubmed CrossRef
  5. Cordes H, Boas U, Olsen P, Heegaard PMH. 2007. Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge. Biomacromolecules 8: 3578-3583.
    Pubmed CrossRef
  6. Supattapone S, Nguyen H-OB, Cohen FE, Prusiner SB, Scott MR. 1999. Elimination of prions by branched polyamines and implications for therapeutics. Proc. Natl. Acad. Sci. USA 96:14529-14534.
    Pubmed CrossRef
  7. Supattapone S, Wille H, Uyechi L, Safar J, Tremblay P, Szoka FC, et al. 2001. Branched polyamines cure prioninfected neuroblastoma cells. J. Virol. 75: 3453-3461.
    Pubmed PMC CrossRef
  8. Lim Y-b, Mays CE, Kim Y, Titlow WB, Ryou C. 2010. The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity. Biomaterials 31: 2025-2033.
    Pubmed CrossRef
  9. Jackson KS, Yeom J, Han Y, Bae Y, Ryou C. 2013. Preference toward a polylysine enantiomer in inhibiting prions. Amino Acids 44: 993-1000.
    Pubmed CrossRef
  10. Ryou C, Titlow WB, Mays CE, Bae Y, Kim S. 2011. The suppression of prion propagation using poly-l-lysine by targeting plasminogen that stimulates prion protein conversion. Biomaterials 32: 3141-3149.
    Pubmed PMC CrossRef
  11. Titlow WB, Waqas M, Lee J, Cho JY, Lee SY, Kim DH, et al. 2016. Effect of polylysine on scrapie prion protein propagation in spleen during asymptomatic stage of experimental prion disease in mice. J. Microbiol. Biotechnol. 26: 1657-1660.
    Pubmed CrossRef
  12. Waqas M, Lee H-M, Kim J , Telling G, Kim J-K, Kim D-H, et al. 2017. Effect of poly-L-arginine in inhibiting scrapie prion protein of cultured cells. Mol. Cell. Biochem. 428: 57-66.
    Pubmed PMC CrossRef
  13. Waqas M, Jeong W-j, Lee Y-J, Kim D-H, Ryou C, Lim Y-b. 2017. pH-dependent in-cell self-assembly of peptide inhibitors increases the anti-prion activity while decreasing the cytotoxicity. Biomacromolecules 18: 943-950.
    Pubmed CrossRef
  14. Xu Z, Adrover M, Pastore A, Prigent S, Mouthon F, Comoy E, et al. 2011. Mechanistic insights into cellular alteration of prion by poly-D-lysine: the role of H2H3 domain. FASEB J. 25: 3426-3435.
    Pubmed CrossRef
  15. Bond VC, Wold B. 1987. Poly-L-ornithine-mediated transformation of mammalian cells. Mol. Cell. Biol. 7: 22862293.
    CrossRef
  16. Ge H, Tan L, Wu P, Yin Y, Liu X, Meng H, et al. 2015. PolyL-ornithine promotes preferred differentiation of neural stem/progenitor cells via ERK signalling pathway. Sci. Rep. 5: 15535.
    Pubmed PMC CrossRef
  17. Lee ES, Na K, Bae YH. 2005. Super pH-sensitive multifunctional polymeric micelle. Nano Lett. 5: 325-329.
    Pubmed CrossRef
  18. Scott MRD, Butler DA, Bredesen DE, Walchli M, Hsiao KK, Prusiner SB. 1988. Prion protein gene expression in cultured cells. Prot. Eng. 2: 69-76.
    Pubmed CrossRef
  19. Arnold JE, Tipler C, Laszlo L, Hope J, Landon M, Mayer RJ. 1995. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176: 403-411.
    Pubmed CrossRef

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Note

J. Microbiol. Biotechnol. 2018; 28(12): 2141-2144

Published online December 28, 2018 https://doi.org/10.4014/jmb.1807.07045

Copyright © The Korean Society for Microbiology and Biotechnology.

Decrease of protease-resistant PrPSc level in ScN2a cells by polyornithine and polyhistidine

Muhammad Waqas 1, Huyen Trang Trinh 1, Sungeun Lee 1, Dae-hwan Kim 1, 2, Sang Yeol Lee 3, Kevin K Choe 1 and Chongsuk Ryou 1*

1Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University, 2School of Undergraduate Studies, Daegu Gyeongbuk Institute of Science and Technology (DGIST), 3Department of Life Science, Gachon University, Seongnam, Gyeonggi-do 13120, Republic of Korea

Received: July 24, 2018; Accepted: October 22, 2018

Abstract

Based on previous studies reporting anti-prion activity of poly-L-lysine and poly-L-arginine, cationic poly-L-ornithine (PLO) and poly-L-histidine (PLH), anionic poly-L-glutamic acid (PLE) and uncharged poly-L-threonine (PLT) were investigated in cultured cells chronically infected by prions to determine anti-prion efficacy. While PLE and PLT did not alter the level of PrPSc, PLO and PLH exhibited potent PrPSc inhibition in ScN2a cells. These results suggest that anti-prion activity of poly-basic amino acids is correlated with cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that anti-prion activity of poly-basic amino acids is associated with the acidic cellular compartments.

Keywords: Prion, polyornithine, polyhistidine, cationic amino acid polymer

References

  1. Prusiner SB. 1998. Prions. Proc. Natl. Acad. Sci. USA 95:13363-13383.
    Pubmed CrossRef
  2. Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim P E, G roth D F, et al. 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
    CrossRef
  3. Aguzzi A, Lakkaraju AKK, Frontzek K. 2018. Toward therapy of human prion diseases. Annu. Rev. Pharmacol. Toxicol. 58: 331-351.
    Pubmed CrossRef
  4. Solassol J, Crozet C, Perrier V, Leclaire J, Beranger F, Caminade A-M, et al. 2004. Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie. J. Gen. Virol. 85: 1791-1799.
    Pubmed CrossRef
  5. Cordes H, Boas U, Olsen P, Heegaard PMH. 2007. Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge. Biomacromolecules 8: 3578-3583.
    Pubmed CrossRef
  6. Supattapone S, Nguyen H-OB, Cohen FE, Prusiner SB, Scott MR. 1999. Elimination of prions by branched polyamines and implications for therapeutics. Proc. Natl. Acad. Sci. USA 96:14529-14534.
    Pubmed CrossRef
  7. Supattapone S, Wille H, Uyechi L, Safar J, Tremblay P, Szoka FC, et al. 2001. Branched polyamines cure prioninfected neuroblastoma cells. J. Virol. 75: 3453-3461.
    Pubmed KoreaMed CrossRef
  8. Lim Y-b, Mays CE, Kim Y, Titlow WB, Ryou C. 2010. The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity. Biomaterials 31: 2025-2033.
    Pubmed CrossRef
  9. Jackson KS, Yeom J, Han Y, Bae Y, Ryou C. 2013. Preference toward a polylysine enantiomer in inhibiting prions. Amino Acids 44: 993-1000.
    Pubmed CrossRef
  10. Ryou C, Titlow WB, Mays CE, Bae Y, Kim S. 2011. The suppression of prion propagation using poly-l-lysine by targeting plasminogen that stimulates prion protein conversion. Biomaterials 32: 3141-3149.
    Pubmed KoreaMed CrossRef
  11. Titlow WB, Waqas M, Lee J, Cho JY, Lee SY, Kim DH, et al. 2016. Effect of polylysine on scrapie prion protein propagation in spleen during asymptomatic stage of experimental prion disease in mice. J. Microbiol. Biotechnol. 26: 1657-1660.
    Pubmed CrossRef
  12. Waqas M, Lee H-M, Kim J , Telling G, Kim J-K, Kim D-H, et al. 2017. Effect of poly-L-arginine in inhibiting scrapie prion protein of cultured cells. Mol. Cell. Biochem. 428: 57-66.
    Pubmed KoreaMed CrossRef
  13. Waqas M, Jeong W-j, Lee Y-J, Kim D-H, Ryou C, Lim Y-b. 2017. pH-dependent in-cell self-assembly of peptide inhibitors increases the anti-prion activity while decreasing the cytotoxicity. Biomacromolecules 18: 943-950.
    Pubmed CrossRef
  14. Xu Z, Adrover M, Pastore A, Prigent S, Mouthon F, Comoy E, et al. 2011. Mechanistic insights into cellular alteration of prion by poly-D-lysine: the role of H2H3 domain. FASEB J. 25: 3426-3435.
    Pubmed CrossRef
  15. Bond VC, Wold B. 1987. Poly-L-ornithine-mediated transformation of mammalian cells. Mol. Cell. Biol. 7: 22862293.
    CrossRef
  16. Ge H, Tan L, Wu P, Yin Y, Liu X, Meng H, et al. 2015. PolyL-ornithine promotes preferred differentiation of neural stem/progenitor cells via ERK signalling pathway. Sci. Rep. 5: 15535.
    Pubmed KoreaMed CrossRef
  17. Lee ES, Na K, Bae YH. 2005. Super pH-sensitive multifunctional polymeric micelle. Nano Lett. 5: 325-329.
    Pubmed CrossRef
  18. Scott MRD, Butler DA, Bredesen DE, Walchli M, Hsiao KK, Prusiner SB. 1988. Prion protein gene expression in cultured cells. Prot. Eng. 2: 69-76.
    Pubmed CrossRef
  19. Arnold JE, Tipler C, Laszlo L, Hope J, Landon M, Mayer RJ. 1995. The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176: 403-411.
    Pubmed CrossRef