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References

  1. Prusiner SB. 1998. Prions. Proc. Natl. Acad. Sci. USA 95: 13363-13383.
    Pubmed PMC CrossRef
  2. Prusiner SB. 1991. Molecular biology of prion diseases. Science 252: 1515-1522.
    Pubmed CrossRef
  3. Rogers M, Yehiely F, Scott M, Prusiner SB. 1993. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl. Acad. Sci. USA 90: 31823186.
    CrossRef
  4. Cohen FE, Pan K-M, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. 1994. Structural clues to prion replication. Science 264: 530-531.
    Pubmed CrossRef
  5. Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, et al. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83: 79-90.
    CrossRef
  6. Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, James TL, et al. 1997. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94:10069-10074.
    Pubmed PMC CrossRef
  7. Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, Bastidas RB, et al. 1997. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273: 614-622.
    Pubmed CrossRef
  8. Zulianello L, Kaneko K, Scott M, Erpel S, Han D, Cohen FE, et al. 2000. Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74: 4351-4360.
    Pubmed PMC CrossRef
  9. Mays CE, Ryou C. 2011. Plasminogen: a cellular protein cofactor for PrPSc propagation. Prion 5: 22-27.
    Pubmed PMC CrossRef
  10. Cohen FE, Prusiner SB. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67: 793-819.
    Pubmed CrossRef
  11. Perrier V, Wallace AC, Kaneko K, Safar J, Prusiner SB, Cohen FE. 2000. Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc. Natl. Acad. Sci. USA 97: 6073-6078.
    Pubmed PMC CrossRef
  12. Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, et al. 2012. Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proc. Natl. Acad. Sci. USA 109: 8546-8551.
    Pubmed PMC CrossRef
  13. Ryou C. 2007. Prions and prion diseases: fundamentals and mechanistic details. J. Microbiol. Biotechnol. 17: 1059-1070.
    Pubmed
  14. Mays CE, Ryou C. 2010. Plasminogen stimulates propagation of protease-resistant prion protein in vitro. FASEB J. 24:5102-5112.
    Pubmed CrossRef
  15. Fischer MB, Roeckl C, Parizek P, Schwarz HP, Aguzzi A. 2000. Binding of disease-associated prion protein to plasminogen. Nature 408: 479-483.
    Pubmed CrossRef
  16. Ryou C, Prusiner SB, Legname G. 2003. Cooperative binding of dominant-negative prion protein to kringle domains. J. Mol. Biol. 329: 323-333.
    CrossRef
  17. Maissen M, Roeckl C, Glatzel M, Goldmann W, Aguzzi A. 2001. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 357: 2026-2028.
    CrossRef
  18. Negredo C, Monks E, S w eeney T. 2 007. A n ovel r eal-time ultrasonic method for prion protein detection using plasminogen as a capture molecule. BMC Biotechnol. 7: 43.
    Pubmed PMC CrossRef
  19. Perrier V, Kaneko K, Safar J, Vergara J, Tremblay P, DeArmond SJ, et al. 2002. Dominant-negative inhibition of prion replication in transgenic mice. Proc. Natl. Acad. Sci. USA 99: 13079-13084.
    Pubmed PMC CrossRef
  20. Shaked Y, Engelstein R, Gabizon R. 2002. The binding of prion proteins to serum components is affected by detergent extraction conditions. J. Neurochem. 82: 1-5.
    Pubmed CrossRef
  21. Shin W, Lee B, Hong S, Ryou C, Kwon M. 2008. Cloning and expression of a prion protein (PrP) gene from Korean bovine (Bos taurus coreanae) and production of rabbit antibovine PrP antibody. Biotechnol. Lett. 30: 1705-1711.
    Pubmed CrossRef
  22. Warrens AN, Jones MD, Lechler RI. 1997. Splicing by overlap extension by PCR using asymmetric amplification:an improved technique for the generation of hybrid proteins of immunological interest. Gene 186: 29-35.
    CrossRef
  23. Mehlhorn I, Groth D, Stockel J, Moffat B, Reilly D, Yansura D, et al. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35: 5528-5537.
    Pubmed CrossRef
  24. Kuwajima K. 1995. Circular dichroism, pp. 115-135. In Shirley BA (ed.). Methods in Molecular Biology: Protein Stability and Folding: Theory and Practice. Humana Press, Totowa. USA.
    Pubmed CrossRef
  25. Choi BR, Lee J, Kim SY, Yim I, Kim EH, Woo HJ. 2013. Prion protein conversion induced by trivalent iron in vesicular trafficking. Biochem. Biophys. Res. Commun. 432:539-544.
    Pubmed CrossRef
  26. Scatchard G. 1949. The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci. 51: 660-672.
    CrossRef
  27. Goldmann W, Hunter N, Smith G, Foster J, Hope J. 1994. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75: 989-995.
    Pubmed CrossRef
  28. Westaway D, Zuliani V, Cooper CM, Da Costa M, Neuman S, Jenny AL, et al. 1994. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev. 8: 959-969.
    Pubmed CrossRef
  29. Clousard C, Beaudry P, Elsen JM, Milan D, Dussaucy M, Bounneau C, et al. 1995. Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie. J. Gen. Virol. 76: 2097-2101.
    Pubmed CrossRef
  30. Bossers A, Schreuder BE, Muileman IH, Belt PB, Smits MA. 1996. PrP genotype contributes to determining survival times of sheep with natural scrapie. J. Gen. Virol. 77: 2669-2673.
    Pubmed CrossRef
  31. Hunter N, Moore L, Hosie BD, Dingwall WS, Greig A. 1997. Association between natural scrapie and PrP genotype in a flock of Suffolk sheep in Scotland. Vet. Rec. 140: 59-63.
    Pubmed CrossRef
  32. Belt PB, Muileman IH, Schreuder BEC, Ruijter JB, Gielkens ALJ, Smits MA. 1995. Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J. Gen. Virol. 76: 509-517.
    Pubmed CrossRef
  33. Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. Lancet 351: 419.
    CrossRef
  34. Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 43: 826-828.
    Pubmed CrossRef
  35. Striebel JF, Race B, Meade-White KD, LaCasse R, Chesebro B. 2011. Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171. PLoS Pathog. 7: e1002275.
    Pubmed PMC CrossRef

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Article

Research article

J. Microbiol. Biotechnol. 2017; 27(5): 1023-1031

Published online May 28, 2017 https://doi.org/10.4014/jmb.1702.02029

Copyright © The Korean Society for Microbiology and Biotechnology.

Biochemical Analysis of Interaction between Kringle Domains of Plasminogen and Prion Proteins with Q167R Mutation

Jeongmin Lee 1, Byoung Woo Lee 2, Hae-Eun Kang 3, Kevine K. Choe 4, Moosik Kwon 2 and Chongsuk Ryou 4*

1Division of Zoonoses, Center for Immunology and Pathology, National Institute of Health, Korea Centers for Disease Control and Prevention, Cheongwon 28159, Republic of Korea, 2Department of Genetic Engineering, Sungkyunkwan University, Suwon 16419, Republic of Korea, 3Division of Foreign Animal Disease, Animal and Plant Quarantine Agency, Gimcheon 39660, Republic of Korea, 4Department of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University, Ansan 15588, Republic of Korea

Received: February 13, 2017; Accepted: March 8, 2017

Abstract

The conformational change of cellular prion protein (PrPC) to its misfolded counterpart,
termed PrPSc, is mediated by a hypothesized cellular cofactor. This cofactor is believed to
interact directly with certain amino acid residues of PrPC. When these are mutated into
cationic amino acid residues, PrPSc formation and prion replication halt in a dominant negative
(DN) manner, presumably due to strong binding of the cofactor to mutated PrPC, designated
as DN PrP mutants. Previous studies demonstrated that plasminogen and its kringle domains
bind to PrP and accelerate PrPSc generation. In this study, in vitro binding analysis of kringle
domains of plasminogen to Q167R DN mutant PrP (PrPQ167R) was performed in parallel with
the wild type (WT) and Q218K DN mutant PrP (PrPQ218K). The binding affinity of PrPQ167R
was higher than that of WT PrP, but lower than that of PrPQ218K. Scatchard analysis further
indicated that, like PrPQ218K and WT PrP, PrPQ167R interaction with plasminogen occurred
at multiple sites, suggesting cooperativity in this interaction. Competitive binding analysis
using L-lysine or L-arginine confirmed the increase of the specificity and binding affinity of the
interaction as PrP acquired DN mutations. Circular dichroism spectroscopy demonstrated that
the recombinant PrPs used in this study retained the α-helix-rich structure. The α-helix
unfolding study revealed similar conformational stability for WT and DN-mutated PrPs. This
study provides an additional piece of biochemical evidence concerning the interaction of
plasminogen with DN mutant PrPs.

Keywords: prion protein, dominant negative mutant, cofactor, plasminogen

References

  1. Prusiner SB. 1998. Prions. Proc. Natl. Acad. Sci. USA 95: 13363-13383.
    Pubmed KoreaMed CrossRef
  2. Prusiner SB. 1991. Molecular biology of prion diseases. Science 252: 1515-1522.
    Pubmed CrossRef
  3. Rogers M, Yehiely F, Scott M, Prusiner SB. 1993. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl. Acad. Sci. USA 90: 31823186.
    CrossRef
  4. Cohen FE, Pan K-M, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. 1994. Structural clues to prion replication. Science 264: 530-531.
    Pubmed CrossRef
  5. Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, et al. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83: 79-90.
    CrossRef
  6. Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, James TL, et al. 1997. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94:10069-10074.
    Pubmed KoreaMed CrossRef
  7. Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, Bastidas RB, et al. 1997. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273: 614-622.
    Pubmed CrossRef
  8. Zulianello L, Kaneko K, Scott M, Erpel S, Han D, Cohen FE, et al. 2000. Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74: 4351-4360.
    Pubmed KoreaMed CrossRef
  9. Mays CE, Ryou C. 2011. Plasminogen: a cellular protein cofactor for PrPSc propagation. Prion 5: 22-27.
    Pubmed KoreaMed CrossRef
  10. Cohen FE, Prusiner SB. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67: 793-819.
    Pubmed CrossRef
  11. Perrier V, Wallace AC, Kaneko K, Safar J, Prusiner SB, Cohen FE. 2000. Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc. Natl. Acad. Sci. USA 97: 6073-6078.
    Pubmed KoreaMed CrossRef
  12. Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, et al. 2012. Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proc. Natl. Acad. Sci. USA 109: 8546-8551.
    Pubmed KoreaMed CrossRef
  13. Ryou C. 2007. Prions and prion diseases: fundamentals and mechanistic details. J. Microbiol. Biotechnol. 17: 1059-1070.
    Pubmed
  14. Mays CE, Ryou C. 2010. Plasminogen stimulates propagation of protease-resistant prion protein in vitro. FASEB J. 24:5102-5112.
    Pubmed CrossRef
  15. Fischer MB, Roeckl C, Parizek P, Schwarz HP, Aguzzi A. 2000. Binding of disease-associated prion protein to plasminogen. Nature 408: 479-483.
    Pubmed CrossRef
  16. Ryou C, Prusiner SB, Legname G. 2003. Cooperative binding of dominant-negative prion protein to kringle domains. J. Mol. Biol. 329: 323-333.
    CrossRef
  17. Maissen M, Roeckl C, Glatzel M, Goldmann W, Aguzzi A. 2001. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 357: 2026-2028.
    CrossRef
  18. Negredo C, Monks E, S w eeney T. 2 007. A n ovel r eal-time ultrasonic method for prion protein detection using plasminogen as a capture molecule. BMC Biotechnol. 7: 43.
    Pubmed KoreaMed CrossRef
  19. Perrier V, Kaneko K, Safar J, Vergara J, Tremblay P, DeArmond SJ, et al. 2002. Dominant-negative inhibition of prion replication in transgenic mice. Proc. Natl. Acad. Sci. USA 99: 13079-13084.
    Pubmed KoreaMed CrossRef
  20. Shaked Y, Engelstein R, Gabizon R. 2002. The binding of prion proteins to serum components is affected by detergent extraction conditions. J. Neurochem. 82: 1-5.
    Pubmed CrossRef
  21. Shin W, Lee B, Hong S, Ryou C, Kwon M. 2008. Cloning and expression of a prion protein (PrP) gene from Korean bovine (Bos taurus coreanae) and production of rabbit antibovine PrP antibody. Biotechnol. Lett. 30: 1705-1711.
    Pubmed CrossRef
  22. Warrens AN, Jones MD, Lechler RI. 1997. Splicing by overlap extension by PCR using asymmetric amplification:an improved technique for the generation of hybrid proteins of immunological interest. Gene 186: 29-35.
    CrossRef
  23. Mehlhorn I, Groth D, Stockel J, Moffat B, Reilly D, Yansura D, et al. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35: 5528-5537.
    Pubmed CrossRef
  24. Kuwajima K. 1995. Circular dichroism, pp. 115-135. In Shirley BA (ed.). Methods in Molecular Biology: Protein Stability and Folding: Theory and Practice. Humana Press, Totowa. USA.
    Pubmed CrossRef
  25. Choi BR, Lee J, Kim SY, Yim I, Kim EH, Woo HJ. 2013. Prion protein conversion induced by trivalent iron in vesicular trafficking. Biochem. Biophys. Res. Commun. 432:539-544.
    Pubmed CrossRef
  26. Scatchard G. 1949. The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci. 51: 660-672.
    CrossRef
  27. Goldmann W, Hunter N, Smith G, Foster J, Hope J. 1994. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75: 989-995.
    Pubmed CrossRef
  28. Westaway D, Zuliani V, Cooper CM, Da Costa M, Neuman S, Jenny AL, et al. 1994. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev. 8: 959-969.
    Pubmed CrossRef
  29. Clousard C, Beaudry P, Elsen JM, Milan D, Dussaucy M, Bounneau C, et al. 1995. Different allelic effects of the codons 136 and 171 of the prion protein gene in sheep with natural scrapie. J. Gen. Virol. 76: 2097-2101.
    Pubmed CrossRef
  30. Bossers A, Schreuder BE, Muileman IH, Belt PB, Smits MA. 1996. PrP genotype contributes to determining survival times of sheep with natural scrapie. J. Gen. Virol. 77: 2669-2673.
    Pubmed CrossRef
  31. Hunter N, Moore L, Hosie BD, Dingwall WS, Greig A. 1997. Association between natural scrapie and PrP genotype in a flock of Suffolk sheep in Scotland. Vet. Rec. 140: 59-63.
    Pubmed CrossRef
  32. Belt PB, Muileman IH, Schreuder BEC, Ruijter JB, Gielkens ALJ, Smits MA. 1995. Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J. Gen. Virol. 76: 509-517.
    Pubmed CrossRef
  33. Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. Lancet 351: 419.
    CrossRef
  34. Shibuya S, Higuchi J, Shin R-W, Tateishi J, Kitamoto T. 1998. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 43: 826-828.
    Pubmed CrossRef
  35. Striebel JF, Race B, Meade-White KD, LaCasse R, Chesebro B. 2011. Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171. PLoS Pathog. 7: e1002275.
    Pubmed KoreaMed CrossRef