Binding of bovine T194A PrP^C by PrP^Sc-specific antibodies

References

• Hedlin P, Taschuk R, Potter A, Griebel P, Napper S. Detection and Control of Prion Diseases in Food Animals. ISRN Vet Sci 2012; 2012:1 - 24; http://dx.doi.org/10.5402/2012/254739
   Google Scholar
• Beekes M. Prions and prion diseases. FEBS J 2007; 274:575; http://dx.doi.org/10.1111/j.1742-4658.2006.05629.x; PMID: 17288546
   PubMed Web of Science ®Google Scholar
• Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24:519 - 50; http://dx.doi.org/10.1146/annurev.neuro.24.1.519; PMID: 11283320
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; http://dx.doi.org/10.1126/science.6801762; PMID: 6801762
   PubMed Web of Science ®Google Scholar
• Prusiner SB. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 2012; 336:1511 - 3; http://dx.doi.org/10.1126/science.1222951; PMID: 22723400
   PubMed Web of Science ®Google Scholar
• Grad LI, Guest WC, Yanai A, Pokrishevsky E, O’Neill MA, Gibbs E, et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells. Proc Natl Acad Sci U S A 2011; 108:16398 - 403; http://dx.doi.org/10.1073/pnas.1102645108; PMID: 21930926
   PubMed Web of Science ®Google Scholar
• Luk KC, Kehm V, Carroll J, Zhang B, O’Brien P, Trojanowski JQ, et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012; 338:949 - 53; http://dx.doi.org/10.1126/science.1227157; PMID: 23161999
   PubMed Web of Science ®Google Scholar
• Miller G. Neurodegeneration. Could they all be prion diseases?. Science 2009; 326:1337 - 9; http://dx.doi.org/10.1126/science.326.5958.1337; PMID: 19965731
   PubMed Web of Science ®Google Scholar
• Polymenidou M, Cleveland DW. Prion-like spread of protein aggregates in neurodegeneration. J Exp Med 2012; 209:889 - 93; http://dx.doi.org/10.1084/jem.20120741; PMID: 22566400
   PubMed Web of Science ®Google Scholar
• Baron T, Biacabe AG. Origin of bovine spongiform encephalopathy. Lancet 2006; 367:297 - 8, author reply 298-9; http://dx.doi.org/10.1016/S0140-6736(06)68060-4; PMID: 16443028
   PubMed Web of Science ®Google Scholar
• Biacabe AG, Morignat E, Vulin J, Calavas D, Baron TG. Atypical bovine spongiform encephalopathies, France, 2001-2007. Emerg Infect Dis 2008; 14:298 - 300; http://dx.doi.org/10.3201/eid1402.071141; PMID: 18258124
   PubMed Web of Science ®Google Scholar
• Williams ES. Chronic wasting disease. Vet Pathol 2005; 42:530 - 49; http://dx.doi.org/10.1354/vp.42-5-530; PMID: 16145200
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ, Aguzzi A. Chronic wasting disease. Biochim Biophys Acta 2007; 1772:610 - 8; http://dx.doi.org/10.1016/j.bbadis.2006.10.010; PMID: 17223321
   PubMed Web of Science ®Google Scholar
• Li L, Napper S, Cashman NR. Immunotherapy for prion diseases: opportunities and obstacles. Immunotherapy 2010; 2:269 - 82; http://dx.doi.org/10.2217/imt.10.3; PMID: 20635933
   PubMed Web of Science ®Google Scholar
• Mouillet-Richard S, Ermonval M, Chebassier C, Laplanche JL, Lehmann S, Launay JM, et al. Signal transduction through prion protein. Science 2000; 289:1925 - 8; http://dx.doi.org/10.1126/science.289.5486.1925; PMID: 10988071
   PubMed Web of Science ®Google Scholar
• Solforosi L, Criado JR, McGavern DB, Wirz S, Sánchez-Alavez M, Sugama S, et al. Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 2004; 303:1514 - 6; http://dx.doi.org/10.1126/science.1094273; PMID: 14752167
   PubMed Web of Science ®Google Scholar
• Arsenault RJ, Li Y, Potter A, Griebel PJ, Kusalik A, Napper S. Induction of ligand-specific PrP (C) signaling in human neuronal cells. Prion 2012; 6:477 - 88; http://dx.doi.org/10.4161/pri.21914; PMID: 22918447
   PubMed Web of Science ®Google Scholar
• Roettger Y, Du Y, Bacher M, Zerr I, Dodel R, Bach JP. Immunotherapy in prion disease. Nat Rev Neurol 2013; 9:98 - 105; http://dx.doi.org/10.1038/nrneurol.2012.258; PMID: 23247613
   PubMed Web of Science ®Google Scholar
• Paramithiotis E, Pinard M, Lawton T, LaBoissiere S, Leathers VL, Zou WQ, et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 2003; 9:893 - 9; http://dx.doi.org/10.1038/nm883; PMID: 12778138
   PubMed Web of Science ®Google Scholar
• Hedlin PD, Cashman NR, Li L, Gupta J, Babiuk LA, Potter AA, et al. Design and delivery of a cryptic PrP(C) epitope for induction of PrP(Sc)-specific antibody responses. Vaccine 2010; 28:981 - 8; http://dx.doi.org/10.1016/j.vaccine.2009.10.134; PMID: 19925901
   PubMed Web of Science ®Google Scholar
• Coulthart MB, Cashman NR. Variant Creutzfeldt-Jakob disease: a summary of current scientific knowledge in relation to public health. CMAJ 2001; 165:51 - 8; PMID: 11468957
   PubMed Web of Science ®Google Scholar
• Aguzzi A. Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis. J Neurochem 2006; 97:1726 - 39; http://dx.doi.org/10.1111/j.1471-4159.2006.03909.x; PMID: 16805779
   PubMed Web of Science ®Google Scholar
• Hsiao K, Prusiner SB. Inherited human prion diseases. Neurology 1990; 40:1820 - 7; http://dx.doi.org/10.1212/WNL.40.12.1820; PMID: 2247227
   PubMed Web of Science ®Google Scholar
• Windl O, Dempster M, Estibeiro JP, Lathe R, de Silva R, Esmonde T, et al. Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene. Hum Genet 1996; 98:259 - 64; http://dx.doi.org/10.1007/s004390050204; PMID: 8707291
   PubMed Web of Science ®Google Scholar
• Hsiao K, Baker HF, Crow TJ, Poulter M, Owen F, Terwilliger JD, et al. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 1989; 338:342 - 5; http://dx.doi.org/10.1038/338342a0; PMID: 2564168
   PubMed Web of Science ®Google Scholar
• Glatzel M, Ott PM, Linder T, Gebbers JO, Gmür A, Wüst W, et al. Human prion diseases: epidemiology and integrated risk assessment. Lancet Neurol 2003; 2:757 - 63; http://dx.doi.org/10.1016/S1474-4422(03)00588-X; PMID: 14636781
   PubMed Web of Science ®Google Scholar
• Kovács GG, Trabattoni G, Hainfellner JA, Ironside JW, Knight RS, Budka H. Mutations of the prion protein gene phenotypic spectrum. J Neurol 2002; 249:1567 - 82; http://dx.doi.org/10.1007/s00415-002-0896-9; PMID: 12420099
   PubMed Web of Science ®Google Scholar
• Nitrini R, Rosemberg S, Passos-Bueno MR, da Silva LS, Iughetti P, Papadopoulos M, et al. Familial spongiform encephalopathy associated with a novel prion protein gene mutation. Ann Neurol 1997; 42:138 - 46; http://dx.doi.org/10.1002/ana.410420203; PMID: 9266722
   PubMed Web of Science ®Google Scholar
• Finckh U, Müller-Thomsen T, Mann U, Eggers C, Marksteiner J, Meins W, et al. High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes. Am J Hum Genet 2000; 66:110 - 7; http://dx.doi.org/10.1086/302702; PMID: 10631141
   PubMed Web of Science ®Google Scholar
• Kiachopoulos S, Bracher A, Winklhofer KF, Tatzelt J. Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. J Biol Chem 2005; 280:9320 - 9; http://dx.doi.org/10.1074/jbc.M412525200; PMID: 15591591
   PubMed Web of Science ®Google Scholar
• van der Kamp MW, Daggett V. Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding. J Mol Biol 2010; 404:732 - 48; http://dx.doi.org/10.1016/j.jmb.2010.09.060; PMID: 20932979
   PubMed Web of Science ®Google Scholar
• Chebaro Y, Derreumaux P. The conversion of helix H2 to beta-sheet is accelerated in the monomer and dimer of the prion protein upon T183A mutation. J Phys Chem B 2009; 113:6942 - 8; http://dx.doi.org/10.1021/jp900334s; PMID: 19371053
   PubMed Web of Science ®Google Scholar
• Sutherland TC, Long YT, Stefureac RI, Bediako-Amoa I, Kraatz HB, Lee JS. Structure of peptides investigated by nanopore analysis. Nano Lett 2004; 4:1273 - 7; http://dx.doi.org/10.1021/nl049413e
   Web of Science ®Google Scholar
• Stefureac R, Long YT, Kraatz HB, Howard P, Lee JS. Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores. Biochemistry 2006; 45:9172 - 9; http://dx.doi.org/10.1021/bi0604835; PMID: 16866363
   PubMed Web of Science ®Google Scholar
• Madampage CA, Andrievskaia O, Lee JS. Nanopore detection of antibody prion interactions. Anal Biochem 2010; 396:36 - 41; http://dx.doi.org/10.1016/j.ab.2009.08.028; PMID: 19699704
   PubMed Web of Science ®Google Scholar
• Meng H, Detillieux D, Baran C, Krasniqi B, Christensen C, Madampage C, et al. Nanopore analysis of tethered peptides. J Pept Sci 2010; 16:701 - 8; http://dx.doi.org/10.1002/psc.1289; PMID: 20814890
   PubMed Web of Science ®Google Scholar
• Stefureac RI, Madampage CA, Andrievskaia O, Lee JS. Nanopore analysis of the interaction of metal ions with prion proteins and peptides. Biochem Cell Biol 2010; 88:347 - 58; http://dx.doi.org/10.1139/O09-176; PMID: 20453935
   PubMed Web of Science ®Google Scholar
• Madampage CA, Tavassoly O, Christensen C, Kumari M, Lee JS. Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins. Prion 2012; 6:116 - 23; http://dx.doi.org/10.4161/pri.18665; PMID: 22421211
   PubMed Web of Science ®Google Scholar
• Oukhaled G, Mathé J, Biance AL, Bacri L, Betton JM, Lairez D, et al. Unfolding of proteins and long transient conformations detected by single nanopore recording. Phys Rev Lett 2007; 98:158101 - 4; http://dx.doi.org/10.1103/PhysRevLett.98.158101; PMID: 17501386
   PubMed Web of Science ®Google Scholar
• Stefureac R, Waldner L, Howard P, Lee JS. Nanopore analysis of a small 86-residue protein. Small 2008; 4:59 - 63; http://dx.doi.org/10.1002/smll.200700402; PMID: 18058890
   PubMed Web of Science ®Google Scholar
• Baran C, Smith GS, Bamm VV, Harauz G, Lee JS. Divalent cations induce a compaction of intrinsically disordered myelin basic protein. Biochem Biophys Res Commun 2010; 391:224 - 9; http://dx.doi.org/10.1016/j.bbrc.2009.11.036; PMID: 19903451
   PubMed Web of Science ®Google Scholar
• Tavassoly O, Lee JS. Methamphetamine binds to α-synuclein and causes a conformational change which can be detected by nanopore analysis. FEBS Lett 2012; 586:3222 - 8; http://dx.doi.org/10.1016/j.febslet.2012.06.040; PMID: 22771474
   PubMed Web of Science ®Google Scholar
• Baskakov IV, Legname G, Baldwin MA, Prusiner SB, Cohen FE. Pathway complexity of prion protein assembly into amyloid. J Biol Chem 2002; 277:21140 - 8; http://dx.doi.org/10.1074/jbc.M111402200; PMID: 11912192
   PubMed Web of Science ®Google Scholar
• Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K. Prion protein NMR structure and familial human spongiform encephalopathies. Proc Natl Acad Sci U S A 1998; 95:11667 - 72; http://dx.doi.org/10.1073/pnas.95.20.11667; PMID: 9751723
   PubMed Web of Science ®Google Scholar
• López Garcia F, Zahn R, Riek R, Wüthrich K. NMR structure of the bovine prion protein. Proc Natl Acad Sci U S A 2000; 97:8334 - 9; http://dx.doi.org/10.1073/pnas.97.15.8334; PMID: 10899999
   PubMed Web of Science ®Google Scholar
• Southwell AL, Patterson PH. Antibody therapy in neurodegenerative disease. Rev Neurosci 2010; 21:273 - 87; http://dx.doi.org/10.1515/REVNEURO.2010.21.4.273; PMID: 21086760
   PubMed Web of Science ®Google Scholar
• Rakhit R, Robertson J, Vande Velde C, Horne P, Ruth DM, Griffin J, et al. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. Nat Med 2007; 13:754 - 9; http://dx.doi.org/10.1038/nm1559; PMID: 17486090
   PubMed Web of Science ®Google Scholar
• Liu HN, Tjostheim S, Dasilva K, Taylor D, Zhao B, Rakhit R, et al. Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis. J Neurosci 2012; 32:8791 - 9; http://dx.doi.org/10.1523/JNEUROSCI.5053-11.2012; PMID: 22745481
   PubMed Web of Science ®Google Scholar
• Andrievskaia O, McRae H, Elmgren C, Huang H, Balachandran A, Nielsen K. Generation of antibodies against bovine recombinant prion protein in various strains of mice. Clin Vaccine Immunol 2006; 13:98 - 105; http://dx.doi.org/10.1128/CVI.13.1.98-105.2006; PMID: 16426006
   PubMed Web of Science ®Google Scholar