CoChat
Sign Up
Cited by 14Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsAmyloidosis: Diagnosis, Treatment, Outcomes

Transport of prions in the peripheral nervous system: pathways, cell types, and mechanisms

Open access
Koshy, Sam M., Kincaid, Anthony E., Bartz, Jason C.·2022·Viruses
DOI 10.3390/v14030630PMC PMC8954800
Open this paper in CoChat — free accountOpen PDF

Abstract

Prion diseases are transmissible protein misfolding disorders that occur in animals and humans where the endogenous prion protein, PrPC, undergoes a conformational change into self-templating aggregates termed PrPSc. Formation of PrPSc in the central nervous system (CNS) leads to gliosis, spongiosis, and cellular dysfunction that ultimately results in the death of the host. The spread of prions from peripheral inoculation sites to CNS structures occurs through neuroanatomical networks. While it has been established that endogenous PrPC is necessary for prion formation, and that the rate of prion spread is consistent with slow axonal transport, the mechanistic details of PrPSc transport remain elusive. Current research endeavors are primarily focused on the cellular mechanisms of prion transport associated with axons. This includes elucidating specific cell types involved, subcellular machinery, and potential cofactors present during this process.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/v14030630

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 138

  1. [1]Prusiner S.B. Novel proteinaceous infectious particles cause scrapie Science 1982 216 136 144 10.1126/science.6801762 6801762 · DOI
  2. [2]Geschwind M.D. Prion Diseases Contin. (Minneap. Minn.) 2015 21 1612 1638 10.1212/CON.0000000000000251 26633779 PMC4879966 · DOI
  3. [3]Sigurdson C.J. Bartz J.C. Glatzel M. Cellular and Molecular Mechanisms of Prion Disease Annu. Rev. Pathol. Mech. Dis. 2019 14 497 516 10.1146/annurev-pathmechdis-012418-013109 PMC9071098 30355150 · DOI
  4. [4]Cole M. Slow virus diseases Rocky Mt. Intern. Med. 1975 72 294 296 1096280
  5. [5]Fuccillo D.A. Kurent J.E. Sever J.L. Slow virus diseases Annu. Rev. Microbiol. 1974 28 231 234 10.1146/annurev.mi.28.100174.001311 4372938 · DOI
  6. [6]Gajdusek D.C. Slow virus diseases of the central nervous system Am. J. Clin. Pathol. 1971 56 320 332 10.1093/ajcp/56.3.320 4999325 · DOI
  7. [7]Hadlow W.J. Eklund C.M. Scrapie—A virus-induced chronic encephalopathy of sheep Res. Publ. Assoc. Res. Nerv. Ment. Dis. 1968 44 281 306 4978853
  8. [8]Ma J. Wang F. Prion disease and the ‘protein-only hypothesis’ Essays Biochem. 2014 56 181 191 10.1042/bse0560181 25131595 PMC6760854 · DOI
  9. [9]Griffith J.S. Self-replication and scrapie Nature 1967 215 1043 1044 10.1038/2151043a0 4964084 · DOI
  10. [10]Deleault N.R. Harris B.T. Rees J.R. Supattapone S. Formation of native prions from minimal components in vitro Proc. Natl. Acad. Sci. USA 2007 104 9741 9746 10.1073/pnas.0702662104 17535913 PMC1887554 · DOI
  11. [11]Alper T. Haig D.A. Clarke M.C. The scrapie agent: Evidence against its dependence for replication on intrinsic nucleic acid J. Gen. Virol. 1978 41 503 516 10.1099/0022-1317-41-3-503 106090 · DOI
  12. [12]Calzolai L. Lysek D.A. Pérez D.R. Güntert P. Wüthrich K. Prion protein NMR structures of chickens, turtles, and frogs Proc. Natl. Acad. Sci. USA 2005 102 651 655 10.1073/pnas.0408939102 15647366 PMC545536 · DOI
  13. [13]Legname G. Elucidating the function of the prion protein PLoS Pathog. 2017 13 e1006458 10.1371/journal.ppat.1006458 28859171 PMC5578479 · DOI
  14. [14]Fernandez-Funez P. Sanchez-Garcia J. Rincon-Limas D.E. Drosophila models of prionopathies: Insight into prion protein function, transmission, and neurotoxicity Curr. Opin. Genet. Dev. 2017 44 141 148 10.1016/j.gde.2017.03.013 28415023 PMC5474952 · DOI
  15. [15]Vassallo N. Herms J. Cellular prion protein function in copper homeostasis and redox signalling at the synapse J. Neurochem. 2003 86 538 544 10.1046/j.1471-4159.2003.01882.x 12859667 · DOI
  16. [16]Westergard L. Christensen H.M. Harris D.A. The cellular prion protein (PrP(C)): Its physiological function and role in disease Biochim. Biophys. Acta 2007 1772 629 644 10.1016/j.bbadis.2007.02.011 17451912 PMC1986710 · DOI
  17. [17]Ironside J.W. Ritchie D.L. Head M.W. Prion diseases Handb. Clin. Neurol. 2017 145 393 403 10.1016/B978-0-12-802395-2.00028-6 28987186 · DOI
  18. [18]Baldwin K.J. Correll C.M. Prion Disease Semin. Neurol. 2019 39 428 439 10.1055/s-0039-1687841 31533183 · DOI
  19. [19]Pattinson I.H. Resistance of Scrapie Agent to Formalin J. Comp. Pathol. 1965 75 159 164 10.1016/0021-9975(65)90006-X 14317615 · DOI
  20. [20]Dickinson A.G. Taylor D.M. Resistance of scrapie agent to decontamination N. Engl. J. Med. 1978 299 1413 1414 10.1056/NEJM197812212992512 101846 · DOI
  21. [21]Gibbs C.J. Gajdusek D.C. Latarjet R. Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease, and scrapie Proc. Natl. Acad. Sci. USA 1978 75 6268 6270 10.1073/pnas.75.12.6268 104301 PMC393162 · DOI
  22. [22]Brown P. Liberski P.P. Wolff A. Gajdusek D.C. Resistance of scrapie infectivity to steam autoclaving after formaldehyde fixation and limited survival after ashing at 360 degrees C: Practical and theoretical implications J. Infect. Dis. 1990 161 467 472 10.1093/infdis/161.3.467 2107265 · DOI
  23. [23]Caughey B. Raymond G.J. Kocisko D.A. Lansbury P.T. Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies J. Virol. 1997 71 4107 4110 10.1128/jvi.71.5.4107-4110.1997 9094691 PMC191566 · DOI
  24. [24]Yuan Q. Telling G. Bartelt-Hunt S.L. Bartz J.C. Dehydration of Prions on Environmentally Relevant Surfaces Protects Them from Inactivation by Freezing and Thawing J. Virol. 2018 92 e02191-17 10.1128/JVI.02191-17 29386284 PMC5874414 · DOI
  25. [25]Saunders S.E. Yuan Q. Bartz J.C. Bartelt-Hunt S. Effects of solution chemistry and aging time on prion protein adsorption and replication of soil-bound prions PLoS ONE 2011 6 e18752 10.1371/journal.pone.0018752 21526178 PMC3079715 · DOI
  26. [26]Jeffrey M. Goodbrand I.A. Goodsir C.M. Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure Micron 1995 26 277 298 10.1016/0968-4328(95)00004-N 7788281 · DOI
  27. [27]Gajdusek D.C. Zigas V. Studies on the pathogenesis of kuru; a clinical, pathological and epidemiological study of a chronic, progressive, degenerative disease of the central nervous system achieving epidemic proportions among the natives of the Eastern Highlands of New Guinea Klin. Wochenschr. 1958 36 445 459 10.1007/BF01484635 13550856 · DOI
  28. [28]Morales R. Prion strains in mammals: Different conformations leading to disease PLoS Pathog. 2017 13 e1006323 10.1371/journal.ppat.1006323 28683090 PMC5500360 · DOI
  29. [29]Bartz J.C. Prion Strain Diversity Cold Spring Harb. Perspect. Med. 2016 6 a024349 10.1101/cshperspect.a024349 27908925 PMC5131755 · DOI
  30. [30]Hill A.F. Collinge J. Prion strains and species barriers Contrib. Microbiol. 2004 11 33 49 10.1159/000077061 15077403 · DOI
  31. [31]Aguzzi A. Heikenwalder M. Polymenidou M. Insights into prion strains and neurotoxicity Nat. Rev. Mol. Cell Biol. 2007 8 552 561 10.1038/nrm2204 17585315 · DOI
  32. [32]Collinge J. Clarke A.R. A general model of prion strains and their pathogenicity Science 2007 318 930 936 10.1126/science.1138718 17991853 · DOI
  33. [33]Weissmann C. Thoughts on mammalian prion strains Folia Neuropathol. 2009 47 104 113 19618334
  34. [34]Shikiya R.A. Langenfeld K.A. Eckland T.E. Trinh J. Holec S.A.M. Mathiason C.K. Kincaid A.E. Bartz J.C. PrPSc formation and clearance as determinants of prion tropism PLoS Pathog. 2017 13 e1006298 10.1371/journal.ppat.1006298 28355274 PMC5386299 · DOI
  35. [35]Cortez L.M. Nemani S.K. Duque Velásquez C. Sriraman A. Wang Y. Wille H. McKenzie D. Sim V.L. Asymmetric-flow field-flow fractionation of prions reveals a strain-specific continuum of quaternary structures with protease resistance developing at a hydrodynamic radius of 15 nm PLoS Pathog. 2021 17 e1009703 10.1371/journal.ppat.1009703 34181702 PMC8270404 · DOI
  36. [36]Bett C. Lawrence J. Kurt T.D. Orru C. Aguilar-Calvo P. Kincaid A.E. Surewicz W.K. Caughey B. Wu C. Sigurdson C.J. Enhanced neuroinvasion by smaller, soluble prions Acta Neuropathol. Commun. 2017 5 32 10.1186/s40478-017-0430-z 28431576 PMC5399838 · DOI
  37. [37]Hulland T.J. Scrapie and Kuru Can. Vet. J. 1960 1 496 17421260 PMC1585622
  38. [38]Gajdusek D.C. Zigas V. Degenerative disease of the central nervous system in New Guinea; the endemic occurrence of kuru in the native population N. Engl. J. Med. 1957 257 974 978 10.1056/NEJM195711142572005 13483871 · DOI · Paper page
  39. [39]Gajdusek D.C. Zigas V. Kuru; clinical, pathological and epidemiological study of an acute progressive degenerative disease of the central nervous system among natives of the Eastern Highlands of New Guinea Am. J. Med. 1959 26 442 469 10.1016/0002-9343(59)90251-7 13626997 · DOI
  40. [40]Gajdusek D.C. Reid L.H. Studies on kuru. IV. The kuru pattern in Moke, a representative Fore village Am. J. Trop. Med. Hyg. 1961 10 628 638 10.4269/ajtmh.1961.10.628 13702978 · DOI
  41. [41]Gajdusek D.C. Zigas V. Studies on kuru. I. The ethnologic setting of kuru Am. J. Trop. Med. Hyg. 1961 10 80 91 10.4269/ajtmh.1961.10.80 13702980 · DOI
  42. [42]Gajdusek D.C. Zigas V. Baker J. Studies on kuru. III. Patterns of kuru incidence: Demographic and geographic epidemiological analysis Am. J. Trop. Med. Hyg. 1961 10 599 627 10.4269/ajtmh.1961.10.599 13702979 · DOI
  43. [43]Gajdusek D.C. Kuru: An appraisal of five years of investigation Eugen. Q. 1962 9 69 74 10.1080/19485565.1962.9987505 13896277 · DOI
  44. [44]Gajdusek D.C. Kuru Trans. R. Soc. Trop. Med. Hyg. 1963 57 151 169 10.1016/0035-9203(63)90057-9 13946176 · DOI
  45. [46]Wells G.A. Scott A.C. Johnson C.T. Gunning R.F. Hancock R.D. Jeffrey M. Dawson M. Bradley R. A novel progressive spongiform encephalopathy in cattle Vet. Rec. 1987 121 419 420 10.1136/vr.121.18.419 3424605 · DOI
  46. [47]Wilesmith J.W. Wells G.A. Cranwell M.P. Ryan J.B. Bovine spongiform encephalopathy: Epidemiological studies Vet. Rec. 1988 123 638 644 10.1136/vr.128.9.199 3218047 · DOI
  47. [48]Wilesmith J.W. Ryan J.B. Atkinson M.J. Bovine spongiform encephalopathy: Epidemiological studies on the origin Vet. Rec. 1991 128 199 203 10.1136/vr.128.9.199 1823120 · DOI
  48. [49]Bruce M.E. Will R.G. Ironside J.W. McConnell I. Drummond D. Suttie A. McCardle L. Chree A. Hope J. Birkett C. Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent Nature 1997 389 498 501 10.1038/39057 9333239 · DOI
  49. [50]Hill A.F. Desbruslais M. Joiner S. Sidle K.C. Gowland I. Collinge J. Doey L.J. Lantos P. The same prion strain causes vCJD and BSE Nature 1997 389 448 450 10.1038/38925 9333232 · DOI
  50. [51]Houston F. Andréoletti O. Animal prion diseases: The risks to human health Brain Pathol. 2019 29 248 262 10.1111/bpa.12696 30588682 PMC8028554 · DOI
  51. [52]Hartsough G.R. Burger D. Encephalopathy of mink. I. Epizootiologic and clinical observations J. Infect. Dis. 1965 115 387 392 10.1093/infdis/115.4.387 5891240 · DOI
  52. [53]Hanson R.P. Eckroade R.J. Marsh R.F. Zu Rhein G.M. Kanitz C.L. Gustafson D.P. Susceptibility of mink to sheep scrapie Science 1971 172 859 861 10.1126/science.172.3985.859 4102123 · DOI
  53. [54]Marsh R.F. Hanson R.P. On the origin of transmissible mink encephalopathy Slow Transmissible Diseases of the Nervous System Prusiner S.B. Hadlow W.J. Academic Press New York, NY, USA 1979 Volume 1 451 460
  54. [55]Marsh R.F. Bessen R.A. Lehmann S. Hartsough G.R. Epidemiological and experimental studies on a new incident of transmissible mink encephalopathy J. Gen. Virol. 1991 72 Pt 3 589 594 10.1099/0022-1317-72-3-589 1826023 · DOI
  55. [56]Marsh R.F. Bessen R.A. Epidemiologic and experimental studies on transmissible mink encephalopathy Dev. Biol. Stand. 1993 80 111 118 8270100
  56. [57]Baron T. Bencsik A. Biacabe A.G. Morignat E. Bessen R.A. Phenotypic similarity of transmissible mink encephalopathy in cattle and L-type bovine spongiform encephalopathy in a mouse model Emerg. Infect. Dis. 2007 13 1887 1894 10.3201/eid1312.070635 18258040 PMC2876762 · DOI
  57. [58]Adcock J.L. Keiss R.E. Locoism in elk. A disease resembling cerebral pseudolipidosis Bull. Wildl. Dis. Assoc. 1969 5 121 124 10.7589/0090-3558-5.2.121 5816098 · DOI
  58. [59]Williams E.S. Young S. Chronic wasting disease of captive mule deer: A spongiform encephalopathy J. Wildl. Dis. 1980 16 89 98 10.7589/0090-3558-16.1.89 7373730 · DOI
  59. [60]Sigurdson C.J. Aguzzi A. Chronic wasting disease Biochim. Biophys. Acta 2007 1772 610 618 10.1016/j.bbadis.2006.10.010 17223321 PMC2680674 · DOI
  60. [62]Benestad S.L. Mitchell G. Simmons M. Ytrehus B. Vikøren T. First case of chronic wasting disease in Europe in a Norwegian free-ranging reindeer Vet. Res. 2016 47 88 10.1186/s13567-016-0375-4 27641251 PMC5024462 · DOI
  61. [63]Pirisinu L. Tran L. Chiappini B. Vanni I. Di Bari M.A. Vaccari G. Vikøren T. Madslien K.I. Våge J. Spraker T. Novel Type of Chronic Wasting Disease Detected in Moose (Alces alces), Norway Emerg. Infect. Dis. 2018 24 2210 2218 10.3201/eid2412.180702 30457526 PMC6256397 · DOI
  62. [64]Nonno R. Di Bari M.A. Pirisinu L. D’Agostino C. Vanni I. Chiappini B. Marcon S. Riccardi G. Tran L. Vikøren T. Studies in bank voles reveal strain differences between chronic wasting disease prions from Norway and North America Proc. Natl. Acad. Sci. USA 2020 117 31417 31426 10.1073/pnas.2013237117 33229531 PMC7733848 · DOI
  63. [65]Ågren E.O. Sörén K. Gavier-Widén D. Benestad S.L. Tran L. Wall K. Averhed G. Doose N. Våge J. Nöremark M. First Detection of Chronic Wasting Disease in Moose (Alces alces) in Sweden J. Wildl. Dis. 2021 57 461 463 10.7589/JWD-D-20-00141 33822167 · DOI
  64. [66]Güere M.E. Våge J. Tharaldsen H. Kvie K.S. Bårdsen B.J. Benestad S.L. Vikøren T. Madslien K. Rolandsen C.M. Tranulis M.A. Chronic wasting disease in Norway-A survey of prion protein gene variation among cervids Transbound. Emerg. Dis. 2021 1 12 10.1111/tbed.14258 34346562 · DOI
  65. [67]Tranulis M.A. Gavier-Widén D. Våge J. Nöremark M. Korpenfelt S.L. Hautaniemi M. Pirisinu L. Nonno R. Benestad S.L. Chronic wasting disease in Europe: New strains on the horizon Acta Vet. Scand. 2021 63 48 10.1186/s13028-021-00606-x 34823556 PMC8613970 · DOI
  66. [68]Williams E.S. Chronic wasting disease Vet. Pathol. 2005 42 530 549 10.1354/vp.42-5-530 16145200 · DOI
  67. [69]Detwiler L.A. Scrapie Rev. Sci. Tech. 1992 11 491 537 10.20506/rst.11.2.607 1617202 · DOI
  68. [70]Plummer P.J. Scrapie-A Disease of Sheep: A Review of the literature Can. J. Comp. Med. Vet Sci. 1946 10 49 54 21015590
  69. [71]Dickinson A.G. Mackay J.M. Genetical Control of the Incubation Period in Mice of the Neurological Disease, Scrapie Heredity 1964 19 279 288 10.1038/hdy.1964.31 14167576 · DOI
  70. [72]Dickinson A.G. Mackay J.M. Zlotnik I. Transmission by Contact of Scrapie in Mice J. Comp. Pathol. 1964 74 250 254 10.1016/S0368-1742(64)80030-8 14198336 · DOI
  71. [73]Dickinson A.G. Young G.B. Stamp J.T. Renwick C.C. An analysis of natural scrapie in Suffolk sheep Heredity 1965 20 485 503 10.1038/hdy.1965.64 5218169 · DOI
  72. [74]Dickinson A.G. Meikle V.M. Fraser H. Identification of a gene which controls the incubation period of some strains of scrapie agent in mice J. Comp. Pathol. 1968 78 293 299 10.1016/0021-9975(68)90005-4 4970191 · DOI
  73. [75]Dickinson A.G. Stamp J.T. Renwick C.C. Rennie J.C. Some factors controlling the incidence of scrapie in Cheviot sheep injected with a Cheviot-passaged scrapie agent J. Comp. Pathol. 1968 78 313 321 10.1016/0021-9975(68)90007-8 4970193 · DOI
  74. [76]Kimberlin R.H. Biochemical changes in scrapie affeced brain Biochem. J. 1969 114 20P 22P 10.1042/bj1140020P 5817818 PMC1184876 · DOI
  75. [77]Georgsson G. Sigurdarson S. Brown P. Infectious agent of sheep scrapie may persist in the environment for at least 16 years J. Gen. Virol. 2006 87 3737 3740 10.1099/vir.0.82011-0 17098992 · DOI
  76. [78]Saunders S.E. Bartelt-Hunt S.L. Bartz J.C. Prions in the environment: Occurrence, fate and mitigation Prion 2008 2 162 169 10.4161/pri.2.4.7951 19242120 PMC2658766 · DOI
  77. [79]Hawkins S.A. Simmons H.A. Gough K.C. Maddison B.C. Persistence of ovine scrapie infectivity in a farm environment following cleaning and decontamination Vet. Rec. 2015 176 99 10.1136/vr.102743 25362003 · DOI
  78. [80]Andréoletti O. Lacroux C. Chabert A. Monnereau L. Tabouret G. Lantier F. Berthon P. Eychenne F. Lafond-Benestad S. Elsen J.M. PrP(Sc) accumulation in placentas of ewes exposed to natural scrapie: Influence of foetal PrP genotype and effect on ewe-to-lamb transmission J. Gen. Virol. 2002 83 2607 2616 10.1099/0022-1317-83-10-2607 12237445 · DOI
  79. [81]Buyukmihci N. Goehring-Harmon F. Marsh R.F. Neural pathogenesis of experimental scrapie after intraocular inoculation of hamsters Exp. Neurol. 1983 81 396 406 10.1016/0014-4886(83)90271-6 6683661 · DOI
  80. [82]Fraser H. Dickinson A.G. Targeting of scrapie lesions and spread of agent via the retino-tectal projection Brain Res. 1985 346 32 41 10.1016/0006-8993(85)91091-1 4052769 · DOI
  81. [83]Kimberlin R.H. Walker C.A. Pathogenesis of scrapie (strain 263K) in hamsters infected intracerebrally, intraperitoneally or intraocularly J. Gen. Virol. 1986 67 Pt 2 255 263 10.1099/0022-1317-67-2-255 3080549 · DOI
  82. [84]Scott J.R. Davies D. Fraser H. Scrapie in the central nervous system: Neuroanatomical spread of infection and Sinc control of pathogenesis J. Gen. Virol. 1992 73 Pt 7 1637 1644 10.1099/0022-1317-73-7-1637 1629695 · DOI
  83. [85]Scott J.R. Fraser H. Transport and targeting of scrapie infectivity and pathology in the optic nerve projections following intraocular infection Prog. Clin. Biol. Res. 1989 317 645 652 10.1097/00002093-198802030-00158 2513583 · DOI
  84. [86]Sefton A.J. Dreher B. Visual System The Rat Nervous System, Forebrain and Midbrain Paxinos G. Academic Press Inc. Orlando, FL, USA 1985 Volume 1 169 210
  85. [87]Jeffery G. Retinal ganglion cell death and terminal field retraction in the developing rodent visual system Brain Res. 1984 315 81 96 10.1016/0165-3806(84)90079-8 6326969 · DOI
  86. [88]Dreher B. Sefton A.J. Ni S.Y. Nisbett G. The morphology, number, distribution and central projections of Class I retinal ganglion cells in albino and hooded rats Brain Behav. Evol. 1985 26 10 48 10.1159/000118764 3902145 · DOI
  87. [89]Fish S.E. Goodman D.K. Kuo D.C. Polcer J.D. Rhoades R.W. The intercollicular pathway in the golden hamster: An anatomical study J. Comp. Neurol. 1982 204 6 20 10.1002/cne.902040103 7056888 · DOI
  88. [90]Mackay-Sim A. Sefton A.J. Martin P.R. Subcortical projections to lateral geniculate and thalamic reticular nuclei in the hooded rat J. Comp. Neurol. 1983 213 24 35 10.1002/cne.902130103 6826786 · DOI
  89. [91]Hubel D.H. Wiesel T.N. Cortical and callosal connections concerned with the vertical meridian of visual fields in the cat J. Neurophysiol. 1967 30 1561 1573 10.1152/jn.1967.30.6.1561 6066454 · DOI
  90. [92]Kimberlin R.H. Walker C.A. Pathogenesis of mouse scrapie: Dynamics of agent replication in spleen, spinal cord and brain after infection by different routes J. Comp. Pathol. 1979 89 551 562 10.1016/0021-9975(79)90046-X 120379 · DOI
  91. [93]Kimberlin R.H. Walker C.A. Pathogenesis of mouse scrapie: Evidence for neural spread of infection to the CNS J. Gen. Virol. 1980 51 183 187 10.1099/0022-1317-51-1-183 6780656 · DOI
  92. [94]Kimberlin R.H. Walker C.A. The role of the spleen in the neuroinvasion of scrapie in mice Virus Res. 1989 12 201 211 10.1016/0168-1702(89)90039-7 2499134 · DOI
  93. [95]Muramoto T. Kitamoto T. Tateishi J. Goto I. The sequential development of abnormal prion protein accumulation in mice with Creutzfeldt-Jakob disease Am. J. Pathol. 1992 140 1411 1420 1376559 PMC1886534
  94. [96]Brown K.L. Stewart K. Ritchie D.L. Mabbott N.A. Williams A. Fraser H. Morrison W.I. Bruce M.E. Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells Nat. Med. 1999 5 1308 1312 10.1038/15264 10545999 · DOI
  95. [97]Brown K.L. Stewart K. Ritchie D. Fraser H. Morrison W.I. Bruce M.E. Follicular dendritic cells in scrapie pathogenesis Arch. Virol. Suppl. 2000 16 13 21 10.1007/978-3-7091-6308-5_2 11214915 · DOI
  96. [98]Bruce M.E. Brown K.L. Mabbott N.A. Farquhar C.F. Jeffrey M. Follicular dendritic cells in TSE pathogenesis Immunol. Today 2000 21 442 446 10.1016/S0167-5699(00)01696-0 10953096 · DOI
  97. [99]Fraser H. Dickinson A.G. Studies of the lymphoreticular system in the pathogenesis of scrapie: The role of spleen and thymus J. Comp. Pathol. 1978 88 563 573 10.1016/0021-9975(78)90010-5 101558 · DOI
  98. [100]Aguzzi A. Nuvolone M. Zhu C. The immunobiology of prion diseases Nat. Rev. Immunol. 2013 13 888 902 10.1038/nri3553 24189576 · DOI
  99. [101]McCulloch L. Brown K.L. Bradford B.M. Hopkins J. Bailey M. Rajewsky K. Manson J.C. Mabbott N.A. Follicular dendritic cell-specific prion protein (PrP) expression alone is sufficient to sustain prion infection in the spleen PLoS Pathog. 2011 7 e1002402 10.1371/journal.ppat.1002402 22144895 PMC3228802 · DOI
  100. [102]Castro-Seoane R. Hummerich H. Sweeting T. Tattum M.H. Linehan J.M. Fernandez de Marco M. Brandner S. Collinge J. Klöhn P.C. Plasmacytoid dendritic cells sequester high prion titres at early stages of prion infection PLoS Pathog. 2012 8 e1002538 10.1371/journal.ppat.1002538 22359509 PMC3280992 · DOI
  101. [103]Prinz M. Heikenwalder M. Junt T. Schwarz P. Glatzel M. Heppner F.L. Fu Y.X. Lipp M. Aguzzi A. Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion Nature 2003 425 957 962 10.1038/nature02072 14562059 · DOI
  102. [104]Kimberlin R.H. Walker C.A. Pathogenesis of mouse scrapie: Patterns of agent replication in different parts of the CNS following intraperitoneal infection J. R. Soc. Med. 1982 75 618 624 6809940 PMC1438061
  103. [105]Kimberlin R.H. Walker C.A. Pathogenesis of scrapie in mice after intragastric infection Virus Res. 1989 12 213 220 10.1016/0168-1702(89)90040-3 2499135 · DOI
  104. [106]van Keulen L.J. Schreuder B.E. Vromans M.E. Langeveld J.P. Smits M.A. Pathogenesis of natural scrapie in sheep Arch. Virol. Suppl. 2000 16 57 71 10.1007/978-3-7091-6308-5_5 11214935 · DOI
  105. [107]Kaatz M. Fast C. Ziegler U. Balkema-Buschmann A. Hammerschmidt B. Keller M. Oelschlegel A. McIntyre L. Groschup M.H. Spread of classic BSE prions from the gut via the peripheral nervous system to the brain Am. J. Pathol. 2012 181 515 524 10.1016/j.ajpath.2012.05.001 22781833 · DOI
  106. [108]Ackermann I. Ulrich R. Tauscher K. Fatola O.I. Keller M. Shawulu J.C. Arnold M. Czub S. Groschup M.H. Balkema-Buschmann A. Prion Infectivity and PrP Int. J. Mol. Sci. 2021 22 1310 10.3390/ijms222111310 34768738 PMC8583047 · DOI
  107. [109]Hoffmann C. Ziegler U. Buschmann A. Weber A. Kupfer L. Oelschlegel A. Hammerschmidt B. Groschup M.H. Prions spread via the autonomic nervous system from the gut to the central nervous system in cattle incubating bovine spongiform encephalopathy J. Gen. Virol. 2007 88 1048 1055 10.1099/vir.0.82186-0 17325380 · DOI
  108. [110]Beekes M. McBride P.A. Early accumulation of pathological PrP in the enteric nervous system and gut-associated lymphoid tissue of hamsters orally infected with scrapie Neurosci. Lett. 2000 278 181 184 10.1016/S0304-3940(99)00934-9 10653023 · DOI
  109. [111]McBride P.A. Beekes M. Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie Neurosci. Lett. 1999 265 135 138 10.1016/S0304-3940(99)00223-2 10327187 · DOI
  110. [112]Beekes M. Baldauf E. Diringer H. Sequential appearance and accumulation of pathognomonic markers in the central nervous system of hamsters orally infected with scrapie J. Gen. Virol. 1996 77 Pt 8 1925 1934 10.1099/0022-1317-77-8-1925 8760444 · DOI
  111. [113]Beekes M. McBride P.A. Baldauf E. Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie J. Gen. Virol. 1998 79 Pt 3 601 607 10.1099/0022-1317-79-3-601 9519840 · DOI
  112. [114]McBride P.A. Schulz-Schaeffer W.J. Donaldson M. Bruce M. Diringer H. Kretzschmar H.A. Beekes M. Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves J. Virol. 2001 75 9320 9327 10.1128/JVI.75.19.9320-9327.2001 11533195 PMC114500 · DOI
  113. [115]Fox K.A. Jewell J.E. Williams E.S. Miller M.W. Patterns of PrPCWD accumulation during the course of chronic wasting disease infection in orally inoculated mule deer (Odocoileus hemionus) J. Gen. Virol. 2006 87 3451 3461 10.1099/vir.0.81999-0 17030882 · DOI
  114. [116]Sigurdson C.J. Spraker T.R. Miller M.W. Oesch B. Hoover E.A. PrP(CWD) in the myenteric plexus, vagosympathetic trunk and endocrine glands of deer with chronic wasting disease J. Gen. Virol. 2001 82 2327 2334 10.1099/0022-1317-82-10-2327 11562526 · DOI
  115. [117]Kimberlin R.H. Hall S.M. Walker C.A. Pathogenesis of mouse scrapie. Evidence for direct neural spread of infection to the CNS after injection of sciatic nerve J. Neurol. Sci. 1983 61 315 325 10.1016/0022-510X(83)90165-X 6418861 · DOI
  116. [118]Bartz J.C. Kincaid A.E. Bessen R.A. Retrograde transport of transmissible mink encephalopathy within descending motor tracts J. Virol. 2002 76 5759 5768 10.1128/JVI.76.11.5759-5768.2002 11992004 PMC137050 · DOI
  117. [119]Ayers J.I. Kincaid A.E. Bartz J.C. Prion strain targeting independent of strain-specific neuronal tropism J. Virol. 2009 83 81 87 10.1128/JVI.01745-08 18971281 PMC2612296 · DOI
  118. [120]Kratzel C. Mai J. Madela K. Beekes M. Krüger D. Propagation of scrapie in peripheral nerves after footpad infection in normal and neurotoxin exposed hamsters Vet. Res. 2007 38 127 139 10.1051/vetres:2006047 17181988 · DOI
  119. [121]Langenfeld K.A. Shikiya R.A. Kincaid A.E. Bartz J.C. Incongruity between Prion Conversion and Incubation Period following Coinfection J. Virol. 2016 90 5715 5723 10.1128/JVI.00409-16 27053546 PMC4886777 · DOI
  120. [122]Bartz J.C. Kincaid A.E. Bessen R.A. Rapid prion neuroinvasion following tongue infection J. Virol. 2003 77 583 591 10.1128/JVI.77.1.583-591.2003 12477862 PMC140623 · DOI
  121. [123]Davis B.M. Rall G.F. Schnell M.J. Everything You Always Wanted to Know About Rabies Virus (But Were Afraid to Ask) Annu. Rev. Virol. 2015 2 451 471 10.1146/annurev-virology-100114-055157 26958924 PMC6842493 · DOI
  122. [124]Diefenbach R.J. Miranda-Saksena M. Douglas M.W. Cunningham A.L. Transport and egress of herpes simplex virus in neurons Rev. Med. Virol. 2008 18 35 51 10.1002/rmv.560 17992661 · DOI
  123. [125]Follet J. Lemaire-Vieille C. Blanquet-Grossard F. Podevin-Dimster V. Lehmann S. Chauvin J.P. Decavel J.P. Varea R. Grassi J. Fontès M. PrP expression and replication by Schwann cells: Implications in prion spreading J. Virol. 2002 76 2434 2439 10.1128/jvi.76.5.2434-2439.2002 11836421 PMC135945 · DOI
  124. [126]Groschup M.H. Beekes M. McBride P.A. Hardt M. Hainfellner J.A. Budka H. Deposition of disease-associated prion protein involves the peripheral nervous system in experimental scrapie Acta Neuropathol. 1999 98 453 457 10.1007/s004010051108 10541866 · DOI
  125. [127]Hainfellner J.A. Budka H. Disease associated prion protein may deposit in the peripheral nervous system in human transmissible spongiform encephalopathies Acta Neuropathol. 1999 98 458 460 10.1007/s004010051109 10541867 · DOI
  126. [128]Magalhães A.C. Baron G.S. Lee K.S. Steele-Mortimer O. Dorward D. Prado M.A. Caughey B. Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells J. Neurosci. 2005 25 5207 5216 10.1523/JNEUROSCI.0653-05.2005 15917460 PMC6724812 · DOI
  127. [129]Bradford B.M. Tuzi N.L. Feltri M.L. McCorquodale C. Cancellotti E. Manson J.C. Dramatic reduction of PrP C level and glycosylation in peripheral nerves following PrP knock-out from Schwann cells does not prevent transmissible spongiform encephalopathy neuroinvasion J. Neurosci. 2009 29 15445 15454 10.1523/JNEUROSCI.4195-09.2009 20007469 PMC6666120 · DOI
  128. [130]Halliez S. Chesnais N. Mallucci G. Vilotte M. Langevin C. Jaumain E. Laude H. Vilotte J.L. Béringue V. Targeted knock-down of cellular prion protein expression in myelinating Schwann cells does not alter mouse prion pathogenesis J. Gen. Virol. 2013 94 1435 1440 10.1099/vir.0.049619-0 23388201 · DOI
  129. [131]Kovács G.G. Preusser M. Strohschneider M. Budka H. Subcellular localization of disease-associated prion protein in the human brain Am. J. Pathol. 2005 166 287 294 10.1016/S0002-9440(10)62252-3 15632020 PMC1602295 · DOI
  130. [132]Shearin H. Bessen R.A. Axonal and transynaptic spread of prions J. Virol. 2014 88 8640 8655 10.1128/JVI.00378-14 24850738 PMC4135969 · DOI
  131. [133]Maday S. Twelvetrees A.E. Moughamian A.J. Holzbaur E.L. Axonal transport: Cargo-specific mechanisms of motility and regulation Neuron 2014 84 292 309 10.1016/j.neuron.2014.10.019 25374356 PMC4269290 · DOI · Paper page
  132. [134]Goldstein L.S. Yang Z. Microtubule-based transport systems in neurons: The roles of kinesins and dyneins Annu. Rev. Neurosci. 2000 23 39 71 10.1146/annurev.neuro.23.1.39 10845058 · DOI
  133. [135]Büeler H. Aguzzi A. Sailer A. Greiner R.A. Autenried P. Aguet M. Weissmann C. Mice devoid of PrP are resistant to scrapie Cell 1993 73 1339 1347 10.1016/0092-8674(93)90360-3 8100741 · DOI
  134. [136]Prusiner S.B. Groth D. Serban A. Koehler R. Foster D. Torchia M. Burton D. Yang S.L. DeArmond S.J. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies Proc. Natl. Acad. Sci. USA 1993 90 10608 10612 10.1073/pnas.90.22.10608 7902565 PMC47826 · DOI
  135. [137]Brandner S. Raeber A. Sailer A. Blättler T. Fischer M. Weissmann C. Aguzzi A. Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system Proc. Natl. Acad. Sci. USA 1996 93 13148 13151 10.1073/pnas.93.23.13148 8917559 PMC24061 · DOI
  136. [138]Brandner S. Isenmann S. Raeber A. Fischer M. Sailer A. Kobayashi Y. Marino S. Weissmann C. Aguzzi A. Normal host prion protein necessary for scrapie-induced neurotoxicity Nature 1996 379 339 343 10.1038/379339a0 8552188 · DOI
  137. [139]Priola S.A. Cell biology of prion infection Handb. Clin. Neurol. 2018 153 45 68 10.1016/B978-0-444-63945-5.00003-9 29887152 · DOI
  138. [140]Greil C.S. Vorberg I.M. Ward A.E. Meade-White K.D. Harris D.A. Priola S.A. Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent Virology 2008 379 284 293 10.1016/j.virol.2008.07.006 18692214 PMC2614895 · DOI

Cited by

Sorted by citations

Authors
Koshy, S. M., Kincaid, A. E., & Bartz, J. C.
Affiliations
Creighton University (US)
Corresponding author
Bartz, Jason C.
ORCID
Venue
Viruses
Publisher
MDPI AG
Published
2022-03-18
Volume
14
Issue
3
Pages
630
ISSN
1999-4915 (ISSN-L)
DOI
10.3390/v14030630
PMC
PMC8954800
OpenAlex
W4220692513
Cited by
14
References
1
Citations by year
2026: 7 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 1
FWCI
0.18
Type
journal article
Language
en
Open access
Licence
Locations
  • Viruses (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
National Institute of Health (1R01NS107246)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
Keywords
prion disease, peripheral nervous system, axonal transport, prion protein, PrPSc, neurodegeneration, spongiosis, gliosis
MeSH terms
Animals, Central Nervous System, Prions, Prion Diseases, Peripheral Nervous System, PrPSc Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review