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Research Paper

Comparison of 2 synthetically generated recombinant prions

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Pages 215-220 | Received 29 Nov 2013, Accepted 26 Mar 2014, Published online: 10 Apr 2014

References

  • Prusiner SB. Prions. Proc Natl Acad Sci U S A 1998; 95:13363 - 83; http://dx.doi.org/10.1073/pnas.95.23.13363; PMID: 9811807
  • Aguzzi A, Sigurdson C, Heikenwaelder M. Molecular mechanisms of prion pathogenesis. Annu Rev Pathol 2008; 3:11 - 40; http://dx.doi.org/10.1146/annurev.pathmechdis.3.121806.154326; PMID: 18233951
  • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; http://dx.doi.org/10.1126/science.6801762; PMID: 6801762
  • Caughey B, Chesebro B. Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol 1997; 7:56 - 62; http://dx.doi.org/10.1016/S0962-8924(96)10054-4; PMID: 17708907
  • Parchi P, Zou W, Wang W, Brown P, Capellari S, Ghetti B, Kopp N, Schulz-Schaeffer WJ, Kretzschmar HA, Head MW, et al. Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci U S A 2000; 97:10168 - 72; http://dx.doi.org/10.1073/pnas.97.18.10168; PMID: 10963679
  • Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411:810 - 3; http://dx.doi.org/10.1038/35081095; PMID: 11459061
  • Castilla J, Saá P, Morales R, Abid K, Maundrell K, Soto C. Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Methods Enzymol 2006; 412:3 - 21; http://dx.doi.org/10.1016/S0076-6879(06)12001-7; PMID: 17046648
  • Castilla J, Saá P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell 2005; 121:195 - 206; http://dx.doi.org/10.1016/j.cell.2005.02.011; PMID: 15851027
  • Wang F, Wang X, Yuan CG, Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132 - 5; http://dx.doi.org/10.1126/science.1183748; PMID: 20110469
  • Wang F, Zhang Z, Wang X, Li J, Zha L, Yuan CG, Weissmann C, Ma J. Genetic informational RNA is not required for recombinant prion infectivity. J Virol 2012; 86:1874 - 6; http://dx.doi.org/10.1128/JVI.06216-11; PMID: 22090130
  • Zhang Z, Zhang Y, Wang F, Wang X, Xu Y, Yang H, Yu G, Yuan C, Ma J. De novo generation of infectious prions with bacterially expressed recombinant prion protein. FASEB J 2013; 27:4768 - 75; http://dx.doi.org/10.1096/fj.13-233965; PMID: 23970796
  • Kim JI, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, Race B, Qing L, Gambetti P, Caughey B, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 2010; 285:14083 - 7; http://dx.doi.org/10.1074/jbc.C110.113464; PMID: 20304915
  • Deleault NR, Piro JR, Walsh DJ, Wang F, Ma J, Geoghegan JC, Supattapone S. Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids. Proc Natl Acad Sci U S A 2012; 109:8546 - 51; http://dx.doi.org/10.1073/pnas.1204498109; PMID: 22586108
  • Deleault NR, Walsh DJ, Piro JR, Wang F, Wang X, Ma J, Rees JR, Supattapone S. Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions. Proc Natl Acad Sci U S A 2012; 109:E1938 - 46; http://dx.doi.org/10.1073/pnas.1206999109; PMID: 22711839
  • Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A 2007; 104:9741 - 6; http://dx.doi.org/10.1073/pnas.0702662104; PMID: 17535913
  • Geoghegan JC, Miller MB, Kwak AH, Harris BT, Supattapone S. Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor. PLoS Pathog 2009; 5:e1000535; http://dx.doi.org/10.1371/journal.ppat.1000535; PMID: 19649330
  • Gonzalez-Montalban N, Makarava N, Ostapchenko VG, Savtchenk R, Alexeeva I, Rohwer RG, Baskakov IV. Highly efficient protein misfolding cyclic amplification. PLoS Pathog 2011; 7:e1001277; http://dx.doi.org/10.1371/journal.ppat.1001277; PMID: 21347353
  • Imamura M, Kato N, Yoshioka M, Okada H, Iwamaru Y, Shimizu Y, Mohri S, Yokoyama T, Murayama Y. Glycosylphosphatidylinositol anchor-dependent stimulation pathway required for generation of baculovirus-derived recombinant scrapie prion protein. J Virol 2011; 85:2582 - 8; http://dx.doi.org/10.1128/JVI.02098-10; PMID: 21228241
  • Barria MA, Mukherjee A, Gonzalez-Romero D, Morales R, Soto C. De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathog 2009; 5:e1000421; http://dx.doi.org/10.1371/journal.ppat.1000421; PMID: 19436715
  • Polymenidou M, Moos R, Scott M, Sigurdson C, Shi YZ, Yajima B, Hafner-Bratkovic I, Jerala R, Hornemann S, Wuthrich K, et al. The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes. PLoS One 2008; 3:e3872; http://dx.doi.org/10.1371/journal.pone.0003872; PMID: 19060956
  • Baral PK, Wieland B, Swayampakula M, Polymenidou M, Rahman MH, Kav NN, Aguzzi A, James MN. Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1. Acta Crystallogr D Biol Crystallogr 2012; 68:1501 - 12; http://dx.doi.org/10.1107/S0907444912037328; PMID: 23090399
  • Féraudet C, Morel N, Simon S, Volland H, Frobert Y, Créminon C, Vilette D, Lehmann S, Grassi J. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J Biol Chem 2005; 280:11247 - 58; http://dx.doi.org/10.1074/jbc.M407006200; PMID: 15618225
  • Ma J. The role of cofactors in prion propagation and infectivity. PLoS Pathog 2012; 8:e1002589; http://dx.doi.org/10.1371/journal.ppat.1002589; PMID: 22511864
  • Wang F, Ma J. Role of lipid in forming an infectious prion?. Acta Biochim Biophys Sin (Shanghai) 2013; 45:485 - 93; http://dx.doi.org/10.1093/abbs/gmt038; PMID: 23583976
  • Wang F, Yang F, Hu Y, Wang X, Wang X, Jin C, Ma J. Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 2007; 46:7045 - 53; http://dx.doi.org/10.1021/bi700299h; PMID: 17503780
  • Wang F, Yin S, Wang X, Zha L, Sy MS, Ma J. Role of the highly conserved middle region of prion protein (PrP) in PrP-lipid interaction. Biochemistry 2010; 49:8169 - 76; http://dx.doi.org/10.1021/bi101146v; PMID: 20718504
  • Kazlauskaite J, Pinheiro TJ. Aggregation and fibrillization of prions in lipid membranes. Biochem Soc Symp 2005; 211 - 22; PMID: 15649144
  • Kazlauskaite J, Sanghera N, Sylvester I, Vénien-Bryan C, Pinheiro TJ. Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization. Biochemistry 2003; 42:3295 - 304; http://dx.doi.org/10.1021/bi026872q; PMID: 12641461
  • Morillas M, Swietnicki W, Gambetti P, Surewicz WK. Membrane environment alters the conformational structure of the recombinant human prion protein. J Biol Chem 1999; 274:36859 - 65; http://dx.doi.org/10.1074/jbc.274.52.36859; PMID: 10601237
  • Adler V, Zeiler B, Kryukov V, Kascsak R, Rubenstein R, Grossman A. Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro. J Mol Biol 2003; 332:47 - 57; http://dx.doi.org/10.1016/S0022-2836(03)00919-7; PMID: 12946346
  • Gomes MP, Millen TA, Ferreira PS, e Silva NL, Vieira TC, Almeida MS, Silva JL, Cordeiro Y. Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells. J Biol Chem 2008; 283:19616 - 25; http://dx.doi.org/10.1074/jbc.M802102200; PMID: 18456654
  • Li J, Browning S, Mahal SP, Oelschlegel AM, Weissmann C. Darwinian evolution of prions in cell culture. Science 2010; 327:869 - 72; http://dx.doi.org/10.1126/science.1183218; PMID: 20044542
  • Timmes AG, Moore RA, Fischer ER, Priola SA. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PLoS One 2013; 8:e71081; http://dx.doi.org/10.1371/journal.pone.0071081; PMID: 23936256
  • Collinge J, Clarke AR. A general model of prion strains and their pathogenicity. Science 2007; 318:930 - 6; http://dx.doi.org/10.1126/science.1138718; PMID: 17991853
  • Schulz-Schaeffer WJ, Tschöke S, Kranefuss N, Dröse W, Hause-Reitner D, Giese A, Groschup MH, Kretzschmar HA. The paraffin-embedded tissue blot detects PrP(Sc) early in the incubation time in prion diseases. Am J Pathol 2000; 156:51 - 6; http://dx.doi.org/10.1016/S0002-9440(10)64705-0; PMID: 10623653
  • Wang X, Bowers SL, Wang F, Pu XA, Nelson RJ, Ma J. Cytoplasmic prion protein induces forebrain neurotoxicity. Biochim Biophys Acta 2009; 1792:555 - 63; http://dx.doi.org/10.1016/j.bbadis.2009.02.014; PMID: 19281844
  • Wang F, Wang X, Ma J. Conversion of bacterially expressed recombinant prion protein. Methods 2011; 53:208 - 13; http://dx.doi.org/10.1016/j.ymeth.2010.12.013; PMID: 21176786