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Is the prevalent human prion protein 129M/V mutation a living fossil from a Paleolithic panzootic superprion pandemic?

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Pages 2-10 | Received 06 Dec 2013, Accepted 19 Dec 2013, Published online: 07 Jan 2014

References

  • Cobb NJ, Surewicz WK. Prion diseases and their biochemical mechanisms. Biochemistry 2009; 48:2574 - 85; http://dx.doi.org/10.1021/bi900108v; PMID: 19239250
  • 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
  • Mead S. Prion disease genetics. Eur J Hum Genet 2006; 14:273 - 81; http://dx.doi.org/10.1038/sj.ejhg.5201544; PMID: 16391566
  • Owen F, Poulter M, Collinge J, Crow TJ. A codon 129 polymorphism in the PRIP gene. Nucleic Acids Res 1990; 18:3103; http://dx.doi.org/10.1093/nar/18.10.3103; PMID: 1971924
  • Petraroli R, Pocchiari M. Codon 219 polymorphism of PRNP in healthy Caucasians and Creutzfeldt-Jakob disease patients. Am J Hum Genet 1996; 58:888 - 9; PMID: 8644754
  • Palmer MS, Dryden AJ, Hughes JT, Collinge J. Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 1991; 352:340 - 2; http://dx.doi.org/10.1038/352340a0; PMID: 1677164
  • Shibuya S, Higuchi J, Shin RW, Tateishi J, Kitamoto T. Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease. Lancet 1998; 351:419; http://dx.doi.org/10.1016/S0140-6736(05)78358-6; PMID: 9482303
  • Polymenidou M, Stoeck K, Glatzel M, Vey M, Bellon A, Aguzzi A. Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. Lancet Neurol 2005; 4:805 - 14; http://dx.doi.org/10.1016/S1474-4422(05)70225-8; PMID: 16297838
  • Collinge J, Palmer MS, Dryden AJ. Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. Lancet 1991; 337:1441 - 2; http://dx.doi.org/10.1016/0140-6736(91)93128-V; PMID: 1675319
  • Collinge J, Beck J, Campbell T, Estibeiro K, Will RG. Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease. Lancet 1996; 348:56; http://dx.doi.org/10.1016/S0140-6736(05)64378-4; PMID: 8691941
  • Zeidler M, Stewart G, Cousens SN, Estibeiro K, Will RG. Codon 129 genotype and new variant CJD. Lancet 1997; 350:668; http://dx.doi.org/10.1016/S0140-6736(05)63366-1; PMID: 9288076
  • Hill AF, Butterworth RJ, Joiner S, Jackson G, Rossor MN, Thomas DJ, Frosh A, Tolley N, Bell JE, Spencer M, et al. Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet 1999; 353:183 - 9; http://dx.doi.org/10.1016/S0140-6736(98)12075-5; PMID: 9923873
  • Lee HS, Brown P, Cervenáková L, Garruto RM, Alpers MP, Gajdusek DC, Goldfarb LG. Increased susceptibility to Kuru of carriers of the PRNP 129 methionine/methionine genotype. J Infect Dis 2001; 183:192 - 6; http://dx.doi.org/10.1086/317935; PMID: 11120925
  • Mead S, Stumpf MP, Whitfield J, Beck JA, Poulter M, Campbell T, Uphill JB, Goldstein D, Alpers M, Fisher EM, et al. Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics. Science 2003; 300:640 - 3; http://dx.doi.org/10.1126/science.1083320; PMID: 12690204
  • Gill ON, Spencer Y, Richard-Loendt A, Kelly C, Dabaghian R, Boyes L, Linehan J, Simmons M, Webb P, Bellerby P, et al. Prevalent abnormal prion protein in human appendixes after bovine spongiform encephalopathy epizootic: large scale survey. BMJ (Clinical research ed 2013; 347:f5675.
  • Nyström S, Mishra R, Hornemann S, Aguzzi A, Nilsson KP, Hammarström P. Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway. J Biol Chem 2012; 287:25975 - 84; http://dx.doi.org/10.1074/jbc.M112.372136; PMID: 22669942
  • Williams TN, Obaro SK. Sickle cell disease and malaria morbidity: a tale with two tails. Trends Parasitol 2011; 27:315 - 20; http://dx.doi.org/10.1016/j.pt.2011.02.004; PMID: 21429801
  • Aidoo M, Terlouw DJ, Kolczak MS, McElroy PD, ter Kuile FO, Kariuki S, Nahlen BL, Lal AA, Udhayakumar V. Protective effects of the sickle cell gene against malaria morbidity and mortality. Lancet 2002; 359:1311 - 2; http://dx.doi.org/10.1016/S0140-6736(02)08273-9; PMID: 11965279
  • Piel FB, Patil AP, Howes RE, Nyangiri OA, Gething PW, Williams TN, Weatherall DJ, Hay SI. Global distribution of the sickle cell gene and geographical confirmation of the malaria hypothesis. Nat Commun 2010; 1:104; http://dx.doi.org/10.1038/ncomms1104; PMID: 21045822
  • Hammarström P, Jiang X, Hurshman AR, Powers ET, Kelly JW. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc Natl Acad Sci U S A 2002; 99:Suppl 4 16427 - 32; http://dx.doi.org/10.1073/pnas.202495199; PMID: 12351683
  • Sekijima Y, Wiseman RL, Matteson J, Hammarström P, Miller SR, Sawkar AR, Balch WE, Kelly JW. The biological and chemical basis for tissue-selective amyloid disease. Cell 2005; 121:73 - 85; http://dx.doi.org/10.1016/j.cell.2005.01.018; PMID: 15820680
  • Sousa A, Coelho T, Barros J, Sequeiros J. Genetic epidemiology of familial amyloidotic polyneuropathy (FAP)-type I in Póvoa do Varzim and Vila do Conde (north of Portugal). Am J Med Genet 1995; 60:512 - 21; http://dx.doi.org/10.1002/ajmg.1320600606; PMID: 8825887
  • Coelho TCR, Sousa A, Alves IL, Torres MF, Saraiva MJM. Compound heterozygotes of transthyretin Met 30 and transthyretin Met 119 are protected from the devastating effects of familial amyloid polyneuropathy. Neuromuscul Disord 1996; 6:Suppl S20; http://dx.doi.org/10.1016/0960-8966(96)88826-2
  • Hammarström P, Schneider F, Kelly JW. Trans-suppression of misfolding in an amyloid disease. Science 2001; 293:2459 - 62; http://dx.doi.org/10.1126/science.1062245; PMID: 11577236
  • Hammarström P, Wiseman RL, Powers ET, Kelly JW. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 2003; 299:713 - 6; http://dx.doi.org/10.1126/science.1079589; PMID: 12560553
  • Westermark P, Sletten K, Johansson B, Cornwell GG 3rd. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A 1990; 87:2843 - 5; http://dx.doi.org/10.1073/pnas.87.7.2843; PMID: 2320592
  • Hornstrup LS, Frikke-Schmidt R, Nordestgaard BG, Tybjærg-Hansen A. Genetic stabilization of transthyretin, cerebrovascular disease, and life expectancy. Arterioscler Thromb Vasc Biol 2013; 33:1441 - 7; http://dx.doi.org/10.1161/ATVBAHA.113.301273; PMID: 23580146
  • Wopfner F, Weidenhöfer G, Schneider R, von Brunn A, Gilch S, Schwarz TF, Werner T, Schätzl HM. Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 1999; 289:1163 - 78; http://dx.doi.org/10.1006/jmbi.1999.2831; PMID: 10373359
  • Hedrick PW. A heterozygote advantage. Science (New York, NY 2003; 302:57.
  • Büeler H, Raeber A, Sailer A, Fischer M, Aguzzi A, Weissmann C. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol Med 1994; 1:19 - 30; PMID: 8790598
  • Appenzeller T. Human migrations: Eastern odyssey. Nature 2012; 485:24 - 6; http://dx.doi.org/10.1038/485024a; PMID: 22552074
  • Callaway E. Archaeology: Date with history. Nature 2012; 485:27 - 9; http://dx.doi.org/10.1038/485027a; PMID: 22552075
  • Lorenzen ED, Nogués-Bravo D, Orlando L, Weinstock J, Binladen J, Marske KA, Ugan A, Borregaard MK, Gilbert MT, Nielsen R, et al. Species-specific responses of Late Quaternary megafauna to climate and humans. Nature 2011; 479:359 - 64; http://dx.doi.org/10.1038/nature10574; PMID: 22048313
  • MacPhee RD, Marx PA. Humans, hyperdisease and first-contact extinctions. In: Goodman S, Patterson, B.D., ed. Natural Change and Human Impact in Madagascar. Washington D.C.: Smithsonian Press, 1997:169–217.
  • Macphee RD, Greenwood AD. Infectious disease, endangerment, and extinction. Int J Evol Biol 2013; 2013:571939; http://dx.doi.org/10.1155/2013/571939; PMID: 23401844
  • Sigurdson CJ, Miller MW. Other animal prion diseases. Br Med Bull 2003; 66:199 - 212; http://dx.doi.org/10.1093/bmb/66.1.199; PMID: 14522860
  • Imran M, Mahmood S. An overview of animal prion diseases. Virol J 2011; 8:493; http://dx.doi.org/10.1186/1743-422X-8-493; PMID: 22044871
  • Gajdusek DC, ed. Nobel Lecture: Unconventional Viruses and the Origin and Disappearance of Kuru. Nobel Media AB: World Scientific Publishing Co, 1976.
  • Williams ES, Kirkwood JK, Miller MW. Transmissible Spongiform Encephalopathies. In: Elizabeth S. Williams, Barker IK, eds. Infectious Diseases of Wild Mammals: Iowa State University Press, Ames, 2001:292-301.
  • Marsh RF, Bessen RA, Lehmann S, Hartsough GR. Epidemiological and experimental studies on a new incident of transmissible mink encephalopathy. J Gen Virol 1991; 72:589 - 94; http://dx.doi.org/10.1099/0022-1317-72-3-589; PMID: 1826023
  • Rothschild BM, Laub R. Hyperdisease in the late Pleistocene: validation of an early 20th century hypothesis. Naturwissenschaften 2006; 93:557 - 64; http://dx.doi.org/10.1007/s00114-006-0144-8; PMID: 16953418
  • Lyons SK, Smith FA, Wagner PJ, White EP, Brown JH. Was a 'hyperdisease' responsible for the late Pleistocene megafaunal extinction?. Ecol Lett 2004; 7:859 - 68; http://dx.doi.org/10.1111/j.1461-0248.2004.00643.x
  • Brown P, Gajdusek DC. Survival of scrapie virus after 3 years’ interment. Lancet 1991; 337:269 - 70; http://dx.doi.org/10.1016/0140-6736(91)90873-N; PMID: 1671114
  • Smith A, Somerville R, Fernie K. TSE infectivity survives burial for five years with little reduction in titer. Prion 2012; 6:138
  • Mead S, Whitfield J, Poulter M, Shah P, Uphill J, Campbell T, Al-Dujaily H, Hummerich H, Beck J, Mein CA, et al. A novel protective prion protein variant that colocalizes with kuru exposure. N Engl J Med 2009; 361:2056 - 65; http://dx.doi.org/10.1056/NEJMoa0809716; PMID: 19923577
  • Baylis M, Goldmann W. The genetics of scrapie in sheep and goats. Curr Mol Med 2004; 4:385 - 96; http://dx.doi.org/10.2174/1566524043360672; PMID: 15354869
  • Nonno R, Di Bari MA, Cardone F, Vaccari G, Fazzi P, Dell’Omo G, Cartoni C, Ingrosso L, Boyle A, Galeno R, et al. Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles. PLoS Pathog 2006; 2:e12; http://dx.doi.org/10.1371/journal.ppat.0020012; PMID: 16518470
  • Agrimi U, Nonno R, Dell’Omo G, Di Bari MA, Conte M, Chiappini B, Esposito E, Di Guardo G, Windl O, Vaccari G, et al. Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles. PLoS Pathog 2008; 4:e1000113; http://dx.doi.org/10.1371/journal.ppat.1000113; PMID: 18654630
  • Heisey DM, Mickelsen NA, Schneider JR, Johnson CJ, Johnson CJ, Langenberg JA, Bochsler PN, Keane DP, Barr DJ. Chronic wasting disease (CWD) susceptibility of several North American rodents that are sympatric with cervid CWD epidemics. J Virol 2010; 84:210 - 5; http://dx.doi.org/10.1128/JVI.00560-09; PMID: 19828611
  • Cartoni C, Schininà ME, Maras B, Nonno R, Vaccari G, Di Baria MA, Conte M, Liu QG, Lu M, Cardone F, et al. Identification of the pathological prion protein allotypes in scrapie-infected heterozygous bank voles (Clethrionomys glareolus) by high-performance liquid chromatography-mass spectrometry. J Chromatogr A 2005; 1081:122 - 6; http://dx.doi.org/10.1016/j.chroma.2005.04.035; PMID: 16013608
  • Lowenstein DH, Butler DA, Westaway D, McKinley MP, DeArmond SJ, Prusiner SB. Three hamster species with different scrapie incubation times and neuropathological features encode distinct prion proteins. Mol Cell Biol 1990; 10:1153 - 63; PMID: 2406562
  • Perucchini M, Griffin K, Miller MW, Goldmann W. PrP genotypes of free-ranging wapiti (Cervus elaphus nelsoni) with chronic wasting disease. J Gen Virol 2008; 89:1324 - 8; http://dx.doi.org/10.1099/vir.0.83424-0; PMID: 18420812
  • Robinson SJ, Samuel MD, O’Rourke KI, Johnson CJ. The role of genetics in chronic wasting disease of North American cervids. Prion 2012; 6:153 - 62; http://dx.doi.org/10.4161/pri.19640; PMID: 22460693
  • Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR, Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011; 470:540 - 2; http://dx.doi.org/10.1038/nature09768; PMID: 21350487
  • Béringue V, Vilotte JL, Laude H. Prion agent diversity and species barrier. Vet Res 2008; 39:47; http://dx.doi.org/10.1051/vetres:2008024; PMID: 18519020
  • Bett C, Kurt TD, Lucero M, Trejo M, Rozemuller AJ, Kong Q, Nilsson KP, Masliah E, Oldstone MB, Sigurdson CJ. Defining the conformational features of anchorless, poorly neuroinvasive prions. PLoS Pathog 2013; 9:e1003280; http://dx.doi.org/10.1371/journal.ppat.1003280; PMID: 23637596
  • Ayers JI, Schutt CR, Shikiya RA, Aguzzi A, Kincaid AE, Bartz JC. The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog 2011; 7:e1001317; http://dx.doi.org/10.1371/journal.ppat.1001317; PMID: 21437239
  • Capobianco R, Casalone C, Suardi S, Mangieri M, Miccolo C, Limido L, Catania M, Rossi G, Di Fede G, Giaccone G, et al. Conversion of the BASE prion strain into the BSE strain: the origin of BSE?. PLoS Pathog 2007; 3:e31; http://dx.doi.org/10.1371/journal.ppat.0030031; PMID: 17352534
  • Brown P, Brandel JP, Sato T, Nakamura Y, MacKenzie J, Will RG, Ladogana A, Pocchiari M, Leschek EW, Schonberger LB. Iatrogenic Creutzfeldt-Jakob disease, final assessment. Emerg Infect Dis 2012; 18:901 - 7; http://dx.doi.org/10.3201/eid1806.120116; PMID: 22607808
  • Almstedt K, Nyström S, Nilsson KP, Hammarström P. Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates. Prion 2009; 3:224 - 35; http://dx.doi.org/10.4161/pri.3.4.10112; PMID: 19923901
  • Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A 2000; 97:145 - 50; http://dx.doi.org/10.1073/pnas.97.1.145; PMID: 10618385
  • Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. Prion protein NMR structures of chickens, turtles, and frogs. Proc Natl Acad Sci U S A 2005; 102:651 - 5; http://dx.doi.org/10.1073/pnas.0408939102; PMID: 15647366