Infectious prions and proteinopathies

REFERENCES

• Prusiner S. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216(4542):136-144; PMID:6801762; http://dx.doi.org/10.1126/science.6801762
   PubMed Web of Science ®Google Scholar
• Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 1982; 218(4579):1309-11; PMID:6815801; http://dx.doi.org/10.1126/science.6815801
   PubMed Web of Science ®Google Scholar
• Safar J, Wille H, Itrri V, Groth D, Serban H, Torchia M, Cohen F.E, Prusiner SB. Eight prion strains have PrPSc molecules with different conformations. Nat Med 1998; 4(10):1157-65; PMID:9771749; http://dx.doi.org/10.1038/2654
   PubMed Web of Science ®Google Scholar
• McKinley MP, Bolton DC, Prusiner S.B. A protease-resistant protein is a structural component of the scrapie prion. Cell 1983; 35(1):57-62; PMID:6414721; http://dx.doi.org/10.1016/0092-8674(83)90207-6
   PubMed Web of Science ®Google Scholar
• Barron RM, Campbell SL, King D, Bellon A, Chapman KE, Williamson RA, Manson JC. High titres of TSE infectivity associated with extremely low levels of PrPSc in vivo. J Biol Chem 2007; 282:35878-886; PMID:17923484; http://dx.doi.org/10.1074/jbc.M704329200
   PubMed Web of Science ®Google Scholar
• Lasmezas CI, Deslys J, Robain O, Jaegly A, Beringue V, Peyrin J, Fournier J, Hauw J, Rossier J, Dormont D. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 1997; 275(5298):402-5; PMID:8994041; http://dx.doi.org/10.1126/science.275.5298.402
   PubMed Web of Science ®Google Scholar
• Piccardo P, Dlouhy SR, Lievens PMJ, Young K, Thomas DP, Nochlin D, Dickson DW, Vinters HV, Zimmerman TR, Mackenzie IRA, et al. Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity. J Neuropathol Exp Neurol 1998; 57(10):979-988; PMID:9786248; http://dx.doi.org/10.1097/00005072-199810000-00010
   PubMed Web of Science ®Google Scholar
• Piccardo P, Manson JC, King D, Ghetti B, Barron RM. Accumulation of prion protein in the brain that is not associated with transmissible disease. Proc Natl Acad Sci U S A 2007; 104(11):4712-17; PMID:17360589; http://dx.doi.org/10.1073/pnas.0609241104
   PubMed Web of Science ®Google Scholar
• Manson JC, Jamieson E, Baybutt H, Tuzi NL, Barron R, McConnell I, Somerville R, Ironside J, Will R, Sy MS, et al. A single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy. EMBO J 1999; 18(23):6855-64; PMID:10581259; http://dx.doi.org/10.1093/emboj/18.23.6855
   PubMed Web of Science ®Google Scholar
• Pirisinu L, Di Bari MA, D'Agostino C, Marcon S, Riccardi G, Poleggi A, Cohen ML, Appleby BS, Gambetti P, Ghetti B, et al. Gerstmann-straussler-scheinker disease subtypes efficiently transmit in bank voles as genuine prion diseases. Scientific Reports 2016; 6:9; PMID:27920429; http://dx.doi.org/10.1038/srep20443
   PubMed Web of Science ®Google Scholar
• Piccardo P, King D, Telling G, Manson JC, Barron RM. Dissociation of prion protein amyloid seeding from transmission of a spongiform encephalopathy. J Virol 2013; 87(22):12349-356; PMID:24027305; http://dx.doi.org/10.1128/JVI.00673-13
   PubMed Web of Science ®Google Scholar
• Fraser H, Dickinson AG. Distribution of experimentally induced scrapie lesions in the brain. Nature 1967; 216:1310-11; PMID:5625087; http://dx.doi.org/10.1038/2161310a0
   PubMed Web of Science ®Google Scholar
• Nazor KE, Kuhn F, Seward T, Green M, Zwald D, Pürro M, Schmid J, Biffiger K, Power AM, Oesch B. et al. Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice. EMBO J 2005; 24(13):2472-80; PMID:15962001; http://dx.doi.org/10.1038/sj.emboj.7600717
   PubMed Web of Science ®Google Scholar
• Barron RM, King D, Jeffrey M, McGovern G, Agarwal S, Gill AC, Piccardo P. PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions. Acta Neuropathol (Berl) 2016; 132(4):1-14; http://dx.doi.org/10.1007/s00401-016-1594-5
   PubMed Web of Science ®Google Scholar
• Makarava N, Savtchenko R, Alexeeva I, Rohwer RG, Baskakov IV. New molecular insight into mechanism of evolution of mammalian synthetic prions. Am J Pathol 2016; 186(4):1006-14; PMID:26873446; http://dx.doi.org/10.1016/j.ajpath.2015.11.013
   PubMed Web of Science ®Google Scholar
• Raymond GJ, Race B, Hollister JR, Offerdahl DK, Moore RA, Kodali R, Raymond LD, Hughson AG, Rosenke R, Long D, et al. Isolation of novel synthetic prion strains by amplification in transgenic mice coexpressing wild-type and anchorless prion proteins. J Virol 2012; 86(21):11763-78; PMID:22915801; http://dx.doi.org/10.1128/JVI.01353-12
   PubMed Web of Science ®Google Scholar
• Colby DW, Wain R, Baskakov IV, Legname G, Palmer CG, Nguyen HOB, Lemus A, Cohen FE, DeArmond SJ, Prusiner SB. Protease-sensitive synthetic prions. Plos Pathog 2010; 6(1):e1000736; PMID:20107515; http://dx.doi.org/10.1371/journal.ppat.1000736
   PubMed Web of Science ®Google Scholar
• Legname G, Baskakov I, Nguyen H, Riesner D, Cohen F, DeArmond S, Prusiner S. Synthetic mammalian prions. Science 2004; 305(5684):673-6; PMID:15286374; http://dx.doi.org/10.1126/science.1100195
   PubMed Web of Science ®Google Scholar
• Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E, Neuenschwander A, Abramowski D, Frey P, Jaton AL, et al. Exogenous induction of cerebral {beta}-Amyloidogenesis is governed by agent and host. Science 2006; 313(5794):1781-84; PMID:16990547; http://dx.doi.org/10.1126/science.1131864
   PubMed Web of Science ®Google Scholar
• Oueslati A, Ximerakis M, Vekrellis K. Protein transmission, seeding and degradation: Key steps for α-synuclein prion-like propagation. Exp Neurobiol 2014; 23(4):324-336; PMID:25548532; http://dx.doi.org/10.5607/en.2014.23.4.324
   PubMedGoogle Scholar
• Ayers JI, Diamond J, Sari A, Fromholt S, Galaleldeen A, Ostrow LW, Glass JD, Hart PJ, Borchelt DR. Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS. Acta Neuropathol 2016; 132(6):827-840; PMID:27704280; http://dx.doi.org/10.1007/s00401-016-1623-4
   PubMed Web of Science ®Google Scholar
• Clavaguera F, Hench J, Goedert M, Tolnay M. Invited review: Prion-like transmission and spreading of tau pathology. Neuropathol Appl Neurobiol 2015; 41(1):47-58; PMID:25399729; http://dx.doi.org/10.1111/nan.12197
   PubMed Web of Science ®Google Scholar
• Jaunmuktane Z, Mead S, Ellis M, Wadsworth JDF, Nicoll AJ, Kenny J, Launchbury F, Linehan J, Richard-Loendt A, Walker AS, et al. Evidence for human transmission of amyloid-[bgr] pathology and cerebral amyloid angiopathy. Nature 2015; 525(7568):247-250; PMID:26354483; http://dx.doi.org/10.1038/nature15369
   PubMed Web of Science ®Google Scholar
• Kovacs GG, Lutz MI, Ricken G, Ströbel T, Höftberger R, Preusser M, Regelsberger G, Hönigschnabl S, Reiner A, Fischer P, et al. Dura mater is a potential source of Aβ seeds. Acta Neuropathol 2016; 131(6):1-13; PMID:26715564; http://dx.doi.org/10.1007/s00401-016-1565-x
   PubMed Web of Science ®Google Scholar
• Irwin DJ, Abrams JY, Schonberger LB, Leschek EW, Mills JL, Lee VMY, Trojanowski JQ. Evaluation of potential infectivity of alzheimer and parkinson disease proteins in recipients of cadaver-derived human growth hormone. Jama Neurol 2013; 70(4):462-8; PMID:23380910; http://dx.doi.org/10.1001/jamaneurol.2013.1933
   PubMed Web of Science ®Google Scholar
• Eisele YS, Bolmont T, Heikenwalder M, Langer F, Jacobson LH, Yan ZX, Roth K, Aguzzi A, Staufenbiel M, Walker LC, et al. Induction of cerebral beta-amyloidosis: Intracerebral versus systemic A beta inoculation. Proc Natl Acad Sci U S A 2009; 106(31):12926-931; PMID:19622727; http://dx.doi.org/10.1073/pnas.0903200106
   PubMed Web of Science ®Google Scholar
• Eisele YS, Duyckaerts C. Propagation of Aß pathology: Hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies. Acta Neuropathol 2016; 131(1):5-25; PMID:26715565; http://dx.doi.org/10.1007/s00401-015-1516-y
   PubMed Web of Science ®Google Scholar
• Jeffrey M, McGovern G, Makarava N, González L, Kim YS, Rohwer RG, Baskakov IV. Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies. Neuropathol Appl Neurobiol 2014; 40(3):296-310; PMID:23578208; http://dx.doi.org/10.1111/nan.12053
   PubMed Web of Science ®Google Scholar
• Jeffrey M, McGovern G, Chambers EV, King D, Gonzalez L, Manson JC, Ghetti B, Piccardo P, Barron RM. Mechanism of PrP-amyloid formation in mice without transmissible spongiform encephalopathy. Brain Pathol 2012; 22(1):58-66; PMID:21645162; http://dx.doi.org/10.1111/j.1750-3639.2011.00508.x
   PubMed Web of Science ®Google Scholar
• Makarava N, Kovacs GG, Bocharova O, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 2010; 119(2):177-187; PMID:20052481; http://dx.doi.org/10.1007/s00401-009-0633-x
   PubMed Web of Science ®Google Scholar
• Klingeborn M, Race B, Meade-White KD, Chesebro B. Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions. Proc Natl Acad Sci U S A 2011; 108(48):E1244-253; PMID:22065744; http://dx.doi.org/10.1073/pnas.1111255108
   PubMed Web of Science ®Google Scholar