In vitro amplification of scrapie and chronic wasting disease PrP^res using baculovirus-expressed recombinant PrP as substrate

References

• Prusiner SB. Prions. Proc Natl Acad Sci 1998; 95:13363-83; http://dx.doi.org/10.1073/pnas.95.23.13363
   PubMed Web of Science ®Google Scholar
• Caughey B, Baron GS, Chesebro B, Jeffrey M. Getting a grip on prions: oligomers, amyloids, anchors and pathological membrane interactions. Annu Rev Biochem 2009; 78:177-204; PMID:19231987; http://dx.doi.org/10.1146/annurev.biochem.78.082907.145410
   PubMed Web of Science ®Google Scholar
• Surewicz WK, Jones EM, Apetri AC. The emerging principles of mammalian prion propagation and transmissibility barriers: insight from studies in vitro. Acc Chem Res 2006; 39:654-62; PMID:16981682; http://dx.doi.org/10.1021/ar050226c
   PubMed Web of Science ®Google Scholar
• Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, Onwubiko HA, Priola SA, Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods 2007; 4:645-50; PMID:17643109; http://dx.doi.org/10.1038/nmeth1066
   PubMed Web of Science ®Google Scholar
• Caughey B. Prions and spongiform encephalopathy (TSE) chemotherapeutics: a common mechanism for anti-TSE compounds? Acc Chem Res 2006; 39:646-53; PMID:16981681; http://dx.doi.org/10.1021/ar050068p
   PubMed Web of Science ®Google Scholar
• Pan KM. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion protein. Proc Natl Acad Sci USA 1993; 90:10962-6; PMID:7902575; http://dx.doi.org/10.1073/pnas.90.23.10962
   PubMed Web of Science ®Google Scholar
• Caughey B, Raymond GJ. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J Biol Chem 1991; 266:18217-23; PMID:1680859
   PubMed Web of Science ®Google Scholar
• Rudd PM, Wormald MR, Wing DR, Prusiner SB, Dwek RA. Prion glycoprotein: structure, dynamics, and roles for the sugars. Biochemistry 2001; 40:3759-66; PMID:11300755; http://dx.doi.org/10.1021/bi002625f
   PubMed Web of Science ®Google Scholar
• Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411:810-3; PMID:11459061; http://dx.doi.org/10.1038/35081095
   PubMed Web of Science ®Google Scholar
• Saa P, Castilla J, Soto C. Presymptomatic detection of prions in blood. Science 2006; 313:92-4; PMID:16825570; http://dx.doi.org/10.1126/science.1129051
   PubMed Web of Science ®Google Scholar
• Soto C, Saborio GP, Anderes L. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Trends Neurosci 2002; 25:390-4; PMID:12127750; http://dx.doi.org/10.1016/S0166-2236(02)02195-1
   PubMed Web of Science ®Google Scholar
• Borchelt DR, Morales R, Stahl N, Telling G, Pruisner SB. Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Glycobiology 1993; 3:319-29; PMID:7691278; http://dx.doi.org/10.1093/glycob/3.4.319
   PubMed Web of Science ®Google Scholar
• Castilla J, Saa P, Soto C. Detection of prions in blood. Nat Med 2005; 11:982-5; PMID:16127436
   PubMed Web of Science ®Google Scholar
• Gonzalez-Romero D, Barria MA, Leon P, Morales R, Soto C. Detection of infectious prions in urine. FEBS letters 2008; 582:3161-6; PMID:18706416; http://dx.doi.org/10.1016/j.febslet.2008.08.003
   PubMed Web of Science ®Google Scholar
• Murayama Y, Yoshioka M, Okada H, Takata M, Yokoyama T, Mohri S. Urinary excretion and blood level of prions in scrapie-infected hamsters. J General Virol 2007; 88:2890-8; PMID:17872544; http://dx.doi.org/10.1099/vir.0.82786-0
   PubMed Web of Science ®Google Scholar
• Thorne L, Terry LA. In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie. J Gen Virol 2008; 89:3177-84; PMID:19008409; http://dx.doi.org/10.1099/vir.0.2008/004226-0
   PubMed Web of Science ®Google Scholar
• Castilla J, Morales R, Saa P, Barria M, Gambetti P, Soto C. Cell-free propagation of prion strains. EMBO J 2008; 27:2557-66; PMID:18800058; http://dx.doi.org/10.1038/emboj.2008.181
   PubMed Web of Science ®Google Scholar
• Green KM, Castilla J, Seward TS, Napier DL, Jewell JE, Soto C, et al. Accelerated high fidelity prion amplification within and across prion species barriers. PLoS Pathog 2008; 4:e1000139; PMID:18769716; http://dx.doi.org/10.1371/journal.ppat.1000139
   PubMed Web of Science ®Google Scholar
• 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; PMID:20304915; http://dx.doi.org/10.1074/jbc.C110.113464
   PubMed Web of Science ®Google Scholar
• Kim J-I, Surewicz K, Gambetti P, Surewicz WK. The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro. FEBS letters 2009; 583:3671-5; PMID:19854187; http://dx.doi.org/10.1016/j.febslet.2009.10.049
   PubMed Web of Science ®Google Scholar
• Kurt TD, Perrott MR, Wilusz CJ, Wilusz J, Supattapone S, Telling GC, Zabel MD, Hoover EA. Efficient in vitro amplification of chronic wasting disease PrPRES. J Virol 2007; 81:9605-8; PMID:17553879; http://dx.doi.org/10.1128/JVI.00635-07
   PubMed Web of Science ®Google Scholar
• Raymond GJ, Bossers A, Raymond LD, O’Rourke KI, McHolland LE, Bryant PK, 3rd, Miller MW, Williams ES, Smits M, Caughey B. Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease. EMBO J 2000; 19:4425-30; PMID:10970836; http://dx.doi.org/10.1093/emboj/19.17.4425
   PubMed Web of Science ®Google Scholar
• Kocisko DA. Cell-free formation of protease-resistant prion protein. Nature 1994; 370:471-4; PMID:7913989; http://dx.doi.org/10.1038/370471a0
   PubMed Web of Science ®Google Scholar
• Kirby L, Birkett CR, Rudyk H, Gilbert IH, Hope J. In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion. J Gen Virol 2003; 84:1013-20; PMID:12655105; http://dx.doi.org/10.1099/vir.0.18903-0
   PubMed Web of Science ®Google Scholar
• Caughey B. Formation of protease-resistant prion protein in cell-free systems. Curr Issues Mol Biol 2000; 2:95-101; PMID:11471561
   PubMedGoogle Scholar
• Wilham JM, Orru CD, Bessen RA, Atarashi R, Sano K, Race B, Meade-White KD, Taubner LM, Timmes A, Caughey B. Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog 2010; 6:e1001217.
   PubMed Web of Science ®Google Scholar
• 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; PMID:21228241; http://dx.doi.org/10.1128/JVI.02098-10
   PubMed Web of Science ®Google Scholar
• Telling GC. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995; 83:79-90; PMID:7553876; http://dx.doi.org/10.1016/0092-8674(95)90236-8
   PubMed Web of Science ®Google Scholar
• Saborio GP. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem Biophys Res Commun 1999; 258:470-5; PMID:10329411; http://dx.doi.org/10.1006/bbrc.1999.0660
   PubMed Web of Science ®Google Scholar
• Stephenson DA, Chiotti K, Ebeling C, Groth D, DeArmond SJ, Prusiner SB, Carlson GA. Quantitative trait loci affecting prion incubation time in mice. Genomics 2000; 69:47-53; PMID:11013074; http://dx.doi.org/10.1006/geno.2000.6320
   PubMed Web of Science ®Google Scholar
• Lloyd SE, Onwuazor ON, Beck JA, Mallinson G, Farrall M, Targonski P, Collinge J, Fisher EM. Identification of multiple quantitative trait loci linked to prion disease incubation period in mice. Proc Natl Acad Sci U S A 2001; 98:6279-83; PMID:11353827; http://dx.doi.org/10.1073/pnas.101130398
   PubMed Web of Science ®Google Scholar
• Manolakou K, Beaton J, McConnell I, Farquar C, Manson J, Hastie ND, Bruce M, Jackson IJ. Genetic and environmental factors modify bovine spongiform encephalopathy incubation period in mice. Proc Natl Acad Sci U S A 2001; 98:7402-7; PMID:11404459; http://dx.doi.org/10.1073/pnas.121172098
   PubMed Web of Science ®Google Scholar
• Deleault NR. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J Biol Chem 2005; 280:26873-9; PMID:15917229; http://dx.doi.org/10.1074/jbc.M503973200
   PubMed Web of Science ®Google Scholar
• Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003; 425:717-20; PMID:14562104; http://dx.doi.org/10.1038/nature01979
   PubMed Web of Science ®Google Scholar
• 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; PMID:12946346; http://dx.doi.org/10.1016/S0022-2836(03)00919-7
   PubMed Web of Science ®Google Scholar
• Gabus C, Derrington E, Leblanc P, Chnaiderman J, Dormont D, Swietnicki W, Swietnicki W, Morillas M, Surewicz WK, Marc D, et al. The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. J Biol Chem 2001; 276:19301-9; PMID:11278562; http://dx.doi.org/10.1074/jbc.M009754200
   PubMed Web of Science ®Google Scholar
• Derrington E, Gabus C, Leblanc P, Chnaidermann J, Grave L, Dormont D, Swietnicki W, Morillas M, Marck D, Nandi P, et al. PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C R Biol 2002; 325:17-23; PMID:11862616; http://dx.doi.org/10.1016/S1631-0691(02)01388-4
   PubMedGoogle Scholar
• Nandi PK, Leclerc E, Nicole JC, Takahashi M. DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J Mol Biol 2002; 322:153-61; PMID:12215421; http://dx.doi.org/10.1016/S0022-2836(02)00750-7
   PubMed Web of Science ®Google Scholar
• Deleault NR, Harris BT, Rees JR, Supattapone S. Formation of native prions from minimal components in vitro. Proceedings of the National Academy of Sciences 2007; 104:9741-6; http://dx.doi.org/10.1073/pnas.0702662104
   PubMed Web of Science ®Google Scholar
• Deleault NR, Kascsak R, Geoghegan JC, Supattapone S. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 2010; 49:3928-34; PMID:20377181; http://dx.doi.org/10.1021/bi100370b
   PubMed Web of Science ®Google Scholar
• Wang F, Wang X, Yuan CG, Ma J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132-5; PMID:20110469; http://dx.doi.org/10.1126/science.1183748
   PubMed Web of Science ®Google Scholar
• Hollister J, Grabenhorst E, Nimtz M, Conradt H, Jarvis DL. Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry 2002; 41:15093-104; PMID:12475259; http://dx.doi.org/10.1021/bi026455d
   PubMed Web of Science ®Google Scholar
• Jarvis DL, Finn EE. Modifying the insect cell N-glycosylation pathway with immediate early baculovirus expression vectors. Nat Biotechnol 1996; 14:1288-92; PMID:9631095; http://dx.doi.org/10.1038/nbt1096-1288
   PubMed Web of Science ®Google Scholar
• Jarvis DL, Kawar ZS, Hollister JR. Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr Opin Biotechnol 1998; 9:528-33; PMID:9821284; http://dx.doi.org/10.1016/S0958-1669(98)80041-4
   PubMedGoogle Scholar
• Priola SA, Lawson VA. Glycosylation influences cross-species formation of protease-resistant prion protein. EMBO J 2001; 20:6692-9; PMID:11726505; http://dx.doi.org/10.1093/emboj/20.23.6692
   PubMed Web of Science ®Google Scholar
• Rudd PM, Merry AH, Wormald MR, Dwek RA. Glycosylation and prion protein. Curr Opin Struct Biol 2002; 12:578-86; PMID:12464308; http://dx.doi.org/10.1016/S0959-440X(02)00377-9
   PubMed Web of Science ®Google Scholar
• Wong C. Sulfated glycans and elevated temperature stimulate PrPSc dependent cell-free formation of protease-resistant prion protein. EMBO J 2001; 20:377-86; PMID:11157745; http://dx.doi.org/10.1093/emboj/20.3.377
   PubMed Web of Science ®Google Scholar
• Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J Biol Chem 2001; 276:14324-8; PMID:11152454; http://dx.doi.org/10.1074/jbc.C100278200
   PubMed Web of Science ®Google Scholar
• Ben-Zaken O. Cellular heparan sulfate participates in the metabolism of prions. J Biol Chem 2003; 278:40041-9; PMID:12871949; http://dx.doi.org/10.1074/jbc.M301152200
   PubMed Web of Science ®Google Scholar
• Weissmann C. A unified theory of prion propagation. Nature 1991; 352:679-83; PMID:1876183; http://dx.doi.org/10.1038/352679a0
   PubMed Web of Science ®Google Scholar
• Choi CJ, Anantharam V, Saetveit NJ, Houk RS, Kanthasamy A, Kanthasamy AG. Normal cellular prion protein protects against manganese-induced oxidative stress and apoptotic cell death. Toxicol Sci 2007; 98:495-509; PMID:17483122; http://dx.doi.org/10.1093/toxsci/kfm099
   PubMed Web of Science ®Google Scholar
• Choi CJ, Anantharam V, Martin DP, Nicholson EM, Richt AJ, Kanthasamy A, Kanthasamy AG. Manganese upregulates cellular prion protein and contributes to altered stabilization and proteolysis: relevance to role of metals in pathogenesis of prion diseases. Toxicol Sci 2010; 115:535-46; PMID:20176619; http://dx.doi.org/10.1093/toxsci/kfq049
   PubMed Web of Science ®Google Scholar
• Choi CJ, Kanthasamy A, Anantharam V, Kanthasamy AG. Interaction of metals with prion protein: possible role of divalent cations in the pathogenesis of prion diseases. Neurotoxicology 2006; 27:777-87; PMID:16860868; http://dx.doi.org/10.1016/j.neuro.2006.06.004
   PubMed Web of Science ®Google Scholar
• Hooper NM, Taylor DR, Watt NT. Mechanism of the metal-mediated endocytosis of the prion protein. Biochem Soc Trans 2008; 36:1272-6; PMID:19021539; http://dx.doi.org/10.1042/BST0361272
   PubMedGoogle Scholar
• Todorova-Balvay D, Simon S, Creminon C, Grassi J, Srikrishnan T, Vijayalakshmi MA. Copper binding to prion octarepeat peptides, a combined metal chelate affinity and immunochemical approaches. J Chromatogr B Analyt Technol Biomed Life Sci 2005; 818:75-82; PMID:15722047; http://dx.doi.org/10.1016/j.jchromb.2004.10.011
   PubMedGoogle Scholar
• Brazier MW, Davies P, Player E, Marken F, Viles JH, Brown DR. Manganese binding to the prion protein. J Biol Chem 2008; 283:12831-9; PMID:18332141; http://dx.doi.org/10.1074/jbc.M709820200
   PubMed Web of Science ®Google Scholar
• Brown DR, Hafiz F, Glasssmith LL, Wong BS, Jones IM, Clive C, Haswell SJ. Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J 2000; 19:1180-6; PMID:10716918; http://dx.doi.org/10.1093/emboj/19.6.1180
   PubMed Web of Science ®Google Scholar
• Brown DR. Brain proteins that mind metals: a neurodegenerative perspective. Dalton Trans 2009:4069-76; PMID:19452053; http://dx.doi.org/10.1039/b822135a
   PubMed Web of Science ®Google Scholar