Prion Diseases of Humans and Animals: Their Causes and Molecular Basis

Collinge, John

doi:10.1146/annurev.neuro.24.1.519

Cited by 1,344Prion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsAmyotrophic Lateral Sclerosis Research

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Prion Diseases of Humans and Animals: Their Causes and Molecular Basis

Collinge, John·2001·Annual Review of Neuroscience

DOI 10.1146/annurev.neuro.24.1.519

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Abstract

Prion diseases are transmissible neurodegenerative conditions that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) and scrapie in animals. Prions appear to be composed principally or entirely of abnormal isoforms of a host-encoded glycoprotein, prion protein. Prion propagation involves recruitment of host cellular prion protein, composed primarily of alpha-helical structure, into a disease specific isoform rich in beta-sheet structure. The existence of multiple prion strains has been difficult to explain in terms of a protein-only infections agent, but recent studies suggest that strain specific phenotypes can be encoded by different prion protein conformations and glycosylation patterns. The ability of a protein to encode phenotypic information has important biological implications. The appearance of a novel human prion disease, variant CJD, and the clear experimental evidence that it is caused by exposure to BSE has highlighted the need to understand the molecular basis of prion propagation, pathogenesis, and the barriers limiting intermammalian transmission. It is unclear if a large epidemic of variant CJD will occur in the years ahead.

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The inherited prion diseases caused by point mutations are generally poorly transmissible, and in some cases not transmissible, to experimental animals and are associated with a molecular type of the disease-associated prion protein (PrP Sc) that is distinct from that of sporadic Creutzfeldt-Jakob disease or kuru.
“The inherited prion diseases caused by point mutations are generally poorly transmissible, and in some cases not transmissible, to experimental animals and are associated with a molecular type of the disease-associated prion protein (PrP Sc ) that is distinct from that of sporadic Creutzfeldt-Jakob disease or kuru.16”
From A Novel Protective Prion Protein Variant that Colocalizes with Kuru Exposure (2009) · cites this paper as [16]

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Research works printed but not linked: 168

Anonymous. 1986. Stabilty constants of metal complexes. In Data for Biochemical Research , ed. RMC Dawson, D Elliot, W Elliot, KM Jones, pp. 399–415. Oxford, UK: Clarendon. 3rd ed.
10.1038/214764a0 · DOI
10.1016/0006-291X(66)90478-5 · DOI
Alpers MP. 1987. Epidemiology and clinical aspects of kuru. SeePrusiner & McKinley 1987, pp. 451–65
10.1038/382779a0 · DOI
10.1002/path.1711760412 · DOI
10.1016/0140-6736(91)92953-Y · DOI
Barlow RM, 1990, Vet. Rec., 126, 111
10.1006/nbdi.1999.0255 · DOI
Beck E, Daniel PM. 1987. Neuropathology of transmissible Spongiform Encephalopathies. SeePrusiner & McKinley 1987, pp. 331–85
10.1016/S0140-6736(77)91958-4 · DOI
10.1038/375698a0 · DOI
Bessen RA, 1992, J. Virol., 66, 2096, 10.1128/jvi.66.4.2096-2101.1992 · DOI
Bessen RA, 1994, J. Virol., 68, 7859, 10.1128/jvi.68.12.7859-7868.1994 · DOI
10.1126/science.6815801 · DOI
10.1083/jcb.110.3.743 · DOI
10.1038/379339a0 · DOI
10.1097/00001756-199410270-00017 · DOI
10.1038/37733 · DOI
10.1006/exnr.1997.6505 · DOI
10.1042/0264-6021:3440001 · DOI
10.1097/00062752-199502060-00012 · DOI
10.1212/WNL.37.6.895 · DOI
10.1098/rstb.1994.0036 · DOI
Bruce ME, Fraser H, McBride PA, Scott JR, Dickinson AG. 1992. The basis of strain variation in scrapie. SeePrusiner et al 1992, pp. 497–508
10.1038/39057 · DOI
10.1016/0092-8674(93)90360-3 · DOI
10.1038/356577a0 · DOI
10.1007/BF03403528 · DOI
10.1016/0092-8674(90)90225-4 · DOI
Caughey B, 1991, J. Biol. Chem., 266, 18217, 10.1016/S0021-9258(18)55257-1 · DOI
10.1016/0304-3940(96)12596-9 · DOI
10.1093/hmg/6.10.1699 · DOI
10.1016/S0140-6736(99)05128-4 · DOI
10.1016/S0140-6736(05)64378-4 · DOI
Collinge J, 1992, Brain, 115, 687
10.1016/S0140-6736(89)90256-0 · DOI
10.1038/3955 · DOI
10.1016/S0140-6736(97)26018-6 · DOI
10.1016/0140-6736(90)91518-F · DOI
10.1016/0140-6736(91)93128-V · DOI · Paper page
10.1016/S0140-6736(95)91405-6 · DOI
10.1038/378779a0 · DOI
10.1016/S0140-6736(96)91407-5 · DOI
10.1038/383685a0 · DOI · Paper page
10.1038/370295a0 · DOI
10.1016/S0140-6736(98)08138-0 · DOI
10.1038/385197a0 · DOI
Cuillé J, 1936, C. R. Acad. Sci., 203, 1552
10.1006/jmbi.1999.3009 · DOI
10.1016/S0896-6273(00)80424-9 · DOI
10.1182/blood.V91.5.1556 · DOI
10.1136/vr.145.6.155 · DOI
10.1099/0022-1317-65-8-1325 · DOI
10.1099/0022-1317-67-3-463 · DOI
10.1002/j.1460-2075.1996.tb00467.x · DOI
10.1038/362543a0 · DOI
10.1126/science.286.5449.2507 · DOI
10.1038/209794a0 · DOI
10.1098/rspb.1998.0596 · DOI
10.1126/science.161.3839.388 · DOI
10.1038/2151043a0 · DOI
10.1016/S0140-6736(59)92081-1 · DOI
10.1073/pnas.90.9.4309 · DOI
10.1523/JNEUROSCI.19-20-08866.1999 · DOI
10.1111/j.1460-9568.1995.tb01049.x · DOI
Herms JW, 1998, Soc. Neurosci. Abstr., 24, 516
10.1099/0022-1317-80-1-11 · DOI
10.1016/S0140-6736(98)12075-5 · DOI
10.1038/38925 · DOI
10.1073/pnas.97.18.10248 · DOI
10.1016/S0304-3940(98)00736-8 · DOI
10.1099/0022-1317-80-1-1 · DOI
10.1073/pnas.95.11.6010 · DOI
10.1006/bbrc.1995.1233 · DOI
10.1006/bbrc.1995.2384 · DOI
10.1038/11507 · DOI
10.1038/338342a0 · DOI
10.1038/ng0492-68 · DOI
10.1126/science.1980379 · DOI
Ingrosso L, 1995, J. Virol., 69, 506, 10.1128/jvi.69.1.506-508.1995 · DOI
10.1126/science.283.5409.1935 · DOI
10.1073/pnas.94.19.10086 · DOI
10.1177/030098588802500514 · DOI
10.1099/0022-1317-34-2-295 · DOI
10.1099/0022-1317-39-3-487 · DOI
10.1099/0022-1317-42-1-107 · DOI
10.1128/AAC.30.3.409 · DOI
Kirkwood JK, 1990, Vet. Rec., 127, 418
Klatzo I, 1959, Lab. Invest., 8, 799
10.1038/4022 · DOI
10.1038/37789 · DOI
10.1159/000110837 · DOI
10.1038/370471a0 · DOI
10.1073/pnas.92.9.3923 · DOI
10.1086/515337 · DOI
10.1016/S0014-5793(99)01123-0 · DOI
10.1016/0169-328X(95)00013-I · DOI
10.1016/0169-328X(95)00323-K · DOI
10.1126/science.275.5298.402 · DOI
10.1002/path.1711660404 · DOI
10.1021/bi982714g · DOI
10.1073/pnas.93.6.2403 · DOI
Manson J, 1992, Development, 115, 117, 10.1242/dev.115.1.117 · DOI
Marsh RF. 1992. Transmissible mink encephalopathy. SeePrusiner et al 1992, pp. 300–307
10.1099/0022-1317-72-3-589 · DOI
10.1093/brain/104.3.559 · DOI
10.1016/0140-6736(92)93224-B · DOI
McGowan JP, 1922, Scott. J. Agric., 5, 365
10.1212/WNL.42.3.669 · DOI
10.1056/NEJM199202133260704 · DOI
10.7589/0090-3558-34.3.532 · DOI
10.1016/0092-8674(91)90384-B · DOI
10.1006/jmbi.1999.3108 · DOI
10.1073/pnas.93.26.15457 · DOI
10.1016/0092-8674(85)90333-2 · DOI
10.1016/S0140-6736(89)91713-3 · DOI
10.1038/352340a0 · DOI · Paper page
10.1073/pnas.90.23.10962 · DOI
10.1038/386232a0 · DOI
10.1002/ana.410390613 · DOI · Paper page
10.1038/230115a0 · DOI
10.1074/jbc.273.50.33107 · DOI
10.1099/0022-1317-68-1-219 · DOI
10.1126/science.6801762 · DOI
10.1126/science.1675487 · DOI
Prusiner SB, 1992, Prion Diseases in Human and Animals.
Prusiner SB, 1987, Prions: Novel Infectious Pathogens Causing Scrapie and Creutzfeldt-Jakob Disease.
10.1016/0092-8674(90)90134-Z · DOI
10.1038/nm1297-1383 · DOI
10.1038/382180a0 · DOI
10.1016/0092-8674(89)90608-9 · DOI
10.1074/jbc.274.25.17981 · DOI
10.1016/S0092-8674(00)81572-X · DOI
10.1083/jcb.125.6.1239 · DOI
Shyng S-L, 1993, J Biol. Chem., 268, 15922, 10.1016/S0021-9258(18)82340-7 · DOI
10.1016/S0140-6736(99)11419-3 · DOI
10.1007/BF01716575 · DOI
10.7589/0090-3558-33.1.1 · DOI
10.1021/bi00059a016 · DOI
10.1021/bi972827k · DOI
10.1016/S0092-8674(00)80596-6 · DOI
10.1074/jbc.272.44.27517 · DOI
10.1126/science.276.5315.1119 · DOI
10.1073/pnas.90.20.9678 · DOI
10.1091/mbc.3.8.851 · DOI
10.1126/science.274.5295.2079 · DOI
10.1016/0092-8674(95)90236-8 · DOI
10.1038/380639a0 · DOI
10.1038/9030 · DOI
10.1074/jbc.275.11.7455 · DOI
10.1038/352679a0 · DOI
10.1136/vr.142.5.103 · DOI
10.1136/vr.121.18.419 · DOI
10.1038/ng0295-197 · DOI
10.1073/pnas.94.19.10012 · DOI
Wickner RB, 1996, Curr. Top. Microbiol. Immunol., 207, 147
10.1038/9323 · DOI
Wilesmith JW, 1988, Vet. Rec., 123, 638
10.1016/S0140-6736(96)91412-9 · DOI
10.1006/jmbi.1996.0343 · DOI
10.1006/exnr.1997.6424 · DOI · Paper page
10.7589/0090-3558-16.1.89 · DOI
10.1016/0378-1119(95)00064-D · DOI
10.1007/s004390050204 · DOI
10.1136/vr.129.11.233 · DOI
10.1016/S0140-6736(97)07472-2 · DOI
10.1007/BF03402121 · DOI

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Authors: Collinge, J.
Affiliations: MRC Prion Unit (GB)
Corresponding author: Collinge, John
ORCID: Collinge, John
Venue: Annual Review of Neuroscience
Publisher: Annual Reviews
Published: 2001-03
Volume: 24
Issue: 1
Pages: 519-550
ISSN: 0147-006X (ISSN-L)
1545-4126
DOI: 10.1146/annurev.neuro.24.1.519
OpenAlex: W2163981524
Cited by: 1,344
References: 0
Citations by year: 2026: 19 · 2025: 28 · 2024: 28 · 2023: 33 · 2022: 34 · 2021: 47 · 2020: 40 · 2019: 45 · 2018: 47 · 2017: 55 · 2016: 53 · 2015: 50 · 2014: 57 · 2013: 73 · 2012: 63
FWCI: 4.43
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Neuroscience (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: prion disease, prion protein, Creutzfeldt-Jakob disease, bovine spongiform encephalopathy, scrapie, variant Creutzfeldt-Jakob disease, prion strains, prion propagation, protein conformation, glycosylation, pathogenesis
MeSH terms: Animals, Cattle, Humans, Creutzfeldt-Jakob Syndrome, Prions, Encephalopathy, Bovine Spongiform, Prion Diseases, Protein Structure, Secondary

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Prion Diseases of Humans and Animals: Their Causes and Molecular Basis

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