OMIA:000944-10036 : Spongiform encephalopathy, susceptibility/resistance to in Mesocricetus auratus (golden hamster)

In other species: Mallard , chicken , Ring-necked pheasant , white-tufted-ear marmoset , macaques , crab-eating macaque , Rhesus monkey , dog , domestic ferret , domestic cat , puma , horse , pig , Arabian camel , deer , Eurasian elk , Western roe deer , red deer , Eastern wapiti , sika deer , Manchurian Wapiti , reindeer , black-tailed deer , white-tailed deer , American bison , taurine cattle , goat , mouflon , sheep , eland , greater kudu , gemsbok , rabbit , domestic guinea pig , domestic yak , chital , fallow deer , cheetah , raccoon dog , bighorn sheep , blue antelope , Arabian oryx , scimitar-horned oryx , nyala , Spanish ibex , water buffalo , Japanese quail , Pyrenean chamois , Iberian red deer , Bank vole , American mink

Categories: Nervous system phene

Possibly relevant human trait(s) and/or gene(s)s (MIM numbers): 176640 (gene) , 245300 (trait)

Links to MONDO diseases:

Mendelian trait/disorder: unknown

Considered a defect: yes

Cross-species summary: Spongiform encephalopathies are a class of fatal neurological diseases. Clinical signs are characteristic of a progressive degeneration of the central nervous system; they include pruritis, abnormalities of gait and recumbency. Death is inevitable. On post-mortem, brain histopathology shows a characteristic spongy appearance. The infectious agent is a modified form of a protein encoded by a gene in the host. The name given to this infectious particle is prion. The host gene is called the prion protein (PrP) gene, which is a normal part of the genome of mammals and chickens. Its polypeptide product, called cellular PrP(superscript C), is a naturally-occurring protein attached to the outer surface of neurones and some other cells. PrP(superscript C) appears to play a role in maintaining the Purkinje cells of the cerebellum, which are essential for balance and muscular function. The infectious agent, called scrapie PrP(superscript Sc), is a modifed form of PrP(superscript C), where the modifications involve glycosylation and the creation of intra-strand di-sulphide bonds. It is important to realise that these modifications involve no change in amino acid sequence. When PrP(superscript Sc) molecules enter a previously uninfected host, they convert the naturally occurring PrP(superscript C) molecules, produced by the host gene, into infectious PrP(superscript Sc) particles, which ultimately cause clinical signs in that animal, and which can spread to other animals, both horizontally (by infection) and vertically (by maternal transmission). In ruminants the disease has been called bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep and goats and chronic wasting disease (CWD) in cervids.

Genetic engineering: Unknown
Have human generated variants been created, e.g. through genetic engineering and gene editing

Cite this entry

Nicholas, F. W., Tammen, I., & Sydney Informatics Hub. (2023). OMIA:000944-10036: Online Mendelian Inheritance in Animals (OMIA) [dataset].


Note: the references are listed in reverse chronological order (from the most recent year to the earliest year), and alphabetically by first author within a year.

2024 Bocharova, O., Makarava, N., Pandit, N.P., Molesworth, K., Baskakov, I.V. :
Multiple steps of prion strain adaptation to a new host. Front Neurosci 18:1329010, 2024. Pubmed reference: 38362022. DOI: 10.3389/fnins.2024.1329010.
2023 Block, A.J., York, T.C., Benedict, R., Ma, J., Bartz, J.C. :
Prion protein amino acid sequence influences formation of authentic synthetic PrP^Sc. Sci Rep 13:441, 2023. Pubmed reference: 36624174. DOI: 10.1038/s41598-022-26300-0.
Bocharova, O., Makarava, N., Pandit, N.P., Molesworth, K., Baskakov, I.V. :
Multiple steps of prion strain adaptation to a new host. bioRxiv , 2023. Pubmed reference: 37961127. DOI: 10.1101/2023.10.24.563743.
Choi, Y.G., Jang, B., Park, J.H., Choi, M.W., Lee, G.Y., Cho, D.J., Kim, H.Y., Lim, H.K., Lee, W.J., Choi, E.K., Kim, Y.S. :
Radotinib decreases prion propagation and prolongs survival times in models of prion disease. Int J Mol Sci 24, 2023. Pubmed reference: 37569615. DOI: 10.3390/ijms241512241.
Šulskis, D., Šneiderienė, G., Žiaunys, M., Smirnovas, V. :
The seeding barrier between human and Syrian hamster prion protein amyloid fibrils is determined by β2-α2 loop sequence elements. Int J Biol Macromol :124038, 2023. Pubmed reference: 36921824. DOI: 10.1016/j.ijbiomac.2023.124038.
2021 Orge, L., Lima, C., Machado, C., Tavares, P., Mendonça, P., Carvalho, P., Silva, J., Pinto, M.L., Bastos, E., Pereira, J.C., Gonçalves-Anjo, N., Gama, A., Esteves, A., Alves, A., Matos, A.C., Seixas, F., Silva, F., Pires, I., Figueira, L., Vieira-Pinto, M., Sargo, R., Pires, M.D.A. :
Neuropathology of animal prion diseases. Biomolecules 11:466, 2021. Pubmed reference: 33801117. DOI: 10.3390/biom11030466.
2004 Hoefert, VB., Aiken, JM., Mckenzie, D., Johnson, CJ. :
Labeling of the scrapie-associated prion protein in vitro and in vivo. Neurosci Lett 371:176-80, 2004. Pubmed reference: 15519752. DOI: 10.1016/j.neulet.2004.08.065.
2002 Kneipp, J., Beekes, M., Lasch, P., Naumann, D. :
Molecular changes of preclinical scrapie can be detected by infrared spectroscopy Journal of Neuroscience 22:2989-2997, 2002. Pubmed reference: 11943801. DOI: 20026226.
Liberski, P.P., Bratosiewicz-Wasik, J., Gajdusek, D.C., Brown, P. :
Ultrastructural studies of experimental scrapie and Creutzfeldt-Jakob disease in hamsters. I. Alterations of myelinated axons Acta Neurobiologiae Experimentalis 62:121-129, 2002. Pubmed reference: 12416389.
Liberski, P.P., Bratosiewiez-Wasik, J., Gajdusek, D.C., Brown, P. :
Ultrastructural studies of experimental scrapie and Creutzfeldt-Jakob disease in hamsters. II. Astrocytic and macrophage reaction towards axonal destruction Acta Neurobiologiae Experimentalis 62:131-139, 2002. Pubmed reference: 12416390.
Schmitt, J., Beekes, M., Brauer, A., Udelhoven, T., Lasch, P., Naumann, D. :
Identification of scrapie infection from blood serum by Fourier transform infrared spectroscopy Analytical Chemistry 74:3865-8, 2002. Pubmed reference: 12175177.
2001 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 Journal of Virology 75:9320-9327, 2001. Pubmed reference: 11533195. DOI: 10.1128/JVI.75.19.9320-9327.2001.
2000 Adjou, K.T., Privat, N., Demart, S., Deslys, J.P., Seman, M., Hauw, J.J., Dormont, D. :
MS-8209, an amphotericin B analogue, delays the appearance of spongiosis, astrogliosis and PrPres accumulation in the brain of scrapie-infected hamsters Journal of Comparative Pathology 122:3-8, 2000. Pubmed reference: 10627386. DOI: 10.1053/jcpa.1999.0338.
Baskakov, I.V., Aagaard, C., Mehlhorn, I., Wille, H., Groth, D., Baldwin, M.A., Prusiner, S.B., Cohen, F.E. :
Self-assembly of recombinant prion protein of 106 residues Biochemistry 39:2792-2804, 2000. Pubmed reference: 10704232.
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 Neuroscience Letters 278:181-184, 2000. Pubmed reference: 10653023.
Hill, A.F., Joiner, S., Linehan, J., Desbruslais, M., Lantos, P.L., Collinge, J. :
Species-barrier-independent prion replication in apparently resistant species Proceedings of the National Academy of Sciences of the United States of America 97:10248-10253, 2000. Pubmed reference: 10963685.
Kimura, K., Kubo, M., Yokoyama, T. :
Characteristics of prion protein (PrPSc) in the brains of hamsters inoculated serially with a mouse-passaged scrapie strain Journal of Comparative Pathology 122:123-130, 2000. Pubmed reference: 10684681. DOI: 10.1053/jcpa.1999.0348.
Parchment, O.G., Essex, J.W. :
Molecular dynamics of mouse and syrian hamster PrP: Implications for activity Proteins: Structure, Function, & Genetics 38:327-340, 2000.
Park, S.K., Choi, S.I., Jin, J.K., Choi, E.K., Kim, J.I., Carp, R.I., Kim, Y.S. :
Differential expression of Bax and Bcl-2 in the brains of hamsters infected with 263K scrapie agent Neuroreport 11:1677-1682, 2000. Pubmed reference: 10852224.
1999 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 Neuropathologica 98:453-457, 1999. Pubmed reference: 10541866.
Kanyo, Z.F., Pan, K.M., Williamson, R.A., Burton, D.R., Prusiner, S.B., Fletterick, R.J., Cohen, F.E. :
Antibody binding defines a structure for an epitope that participates in the PrPC -> PrPSc conformational change Journal of Molecular Biology 293:855-863, 1999. Pubmed reference: 10543972. DOI: 10.1006/jmbi.1999.3193.
McBride, P.A., Beekes, M. :
Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie Neuroscience Letters 265:135-138, 1999. Pubmed reference: 10327187.
Post, K., Riesner, D., Walldorf, V., Mehlhorn, H. :
Fly larvae and pupae as vectors for scrapie Lancet 354:1969-1970, 1999. Pubmed reference: 10622303. DOI: 10.1016/S0140-6736(99)00469-9.
1998 Carlson, G.A. :
Proof of the primacy of prion protein Nature Genetics 18:94-95, 1998. Pubmed reference: 9462729. DOI: 10.1038/ng0298-94.
Dearmond, S.J. :
Changes in the localization of brain prion proteins during scrapie infection - commentary Neurology 50:2, 1998.
Dearmond, S.J., Mobley, W.C., Demott, D.L., Barry, R.A., Beckstead, J.H., Prusiner, S.B. :
Changes in the localization of brain prion proteins during scrapie infection (reprinted from neurology, vol 37, pg 1271-1280, 1987) Neurology 50:A 1-A 10, 1998.
Inouye, H., Kirschner, D.A. :
Polypeptide chain folding in the hydrophobic core of hamster scrapie prion - analysis by x-ray diffraction Journal of Structural Biology 122:247-255, 1998. Pubmed reference: 9724626. DOI: 10.1006/jsbi.1998.3998.
Safar, J., Wille, H., Itrri, V., Groth, D., Serban, H., Torchia, M., Cohen, F.E., Prusiner, S.B. :
Eight prion strains have prpsc molecules with different conformations Nature Medicine 4:1157-1165, 1998. Pubmed reference: 9771749. DOI: 10.1038/2654.
1997 Anon. :
Prion-specific antibody identified Veterinary Record 141:531-532, 1997.
Baldauf, E., Beekes, M., Diringer, H. :
Evidence for an alternative direct route of access for the scrapie agent to the brain bypassing the spinal cord Journal of General Virology 78:1187-1197, 1997. Pubmed reference: 9152440.
Daude, N., Lehmann, S., Harris, D.A. :
Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells Journal of Biological Chemistry 272:11604-11612, 1997. Pubmed reference: 9111077.
Donne, D.G., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Wright, P.E., Dyson, H.J. :
Structure of the recombinant full-length hamster prion protein PRP(29-231) - the n terminus is highly flexible Proceedings of the National Academy of Sciences of the United States of America 94:13452-13457, 1997. Pubmed reference: 9391046.
Glockshuber, R., Hornemann, S., Riek, R., Wider, G., Billeter, M., Wuthrich, K. :
Three-dimensional nmr structure of a self-folding domain of the prion protein PRP(121-231) Trends in Biochemical Sciences 22:241-242, 1997. Pubmed reference: 9255063.
Gregoire, N., Fraser, J.R., Pellissier, J.F., Nicoli, J. :
Synthetic growth hormone has no inducting effect in the development of a prion disease - an experimental study on the scrapie model in hamsters Journal of the Neurological Sciences 152:224-225, 1997. Pubmed reference: 9415545.
James, T.L., Liu, H., Ulyanov, N.B., Farrjones, S., Zhang, H., Donne, D.G., Kaneko, K., Groth, D., Mehlhorn, I., Prusiner, S.B., Cohen, F.E. :
Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform Proceedings of the National Academy of Sciences of the United States of America 94:10086-10091, 1997. Pubmed reference: 9294167.
Kaneko, K., Wille, H., Mehlhorn, I., Zhang, H., Ball, H., Cohen, F.E., Baldwin, M.A., Prusiner, S.B. :
Molecular properties of complexes formed between the prion protein and synthetic peptides Journal of Molecular Biology 270:574-586, 1997. Pubmed reference: 9245588. DOI: 10.1006/jmbi.1997.1135.
Li, G., Bolton, D.C. :
A novel hamster prion protein mRNA contains an extra exon - increased expression in scrapie Brain Research 751:265-274, 1997. Pubmed reference: 9099814.
Liberski, P.P., Brown, P., Cervenakova, L., Gajdusek, D.C. :
Interactions between astrocytes and oligodendroglia in human and experimental creutzfeldt-jakob disease and scrapie Experimental Neurology 144:227-234, 1997. Pubmed reference: 9126175. DOI: 10.1006/exnr.1997.6422.
Naslavsky, N., Stein, R., Yanai, A., Friedlander, G., Taraboulos, A. :
Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform Journal of Biological Chemistry 272:6324-6331, 1997. Pubmed reference: 9045652.
Prusiner, S.B., Scott, M.R. :
Genetics of prions [Review] Annual Review of Genetics 31:139-175, 1997. Pubmed reference: 9442893. DOI: 10.1146/annurev.genet.31.1.139.
Prusiner, S.B. :
Structural biology and genetics of prions Journal of Neurovirology 3:S 21, 1997.
Raeber, A.J., Race, R.E., Brandner, S., Priola, S.A., Sailer, A., Bessen, R.A., Mucke, L., Manson, J., Aguzzi, A., Oldstone, M.B.A., Weissmann, C., Chesebro, B. :
Astrocyte-specific expression of hamster prion protein (prp) renders prp knockout mice susceptible to hamster scrapie EMBO Journal 16:6057-6065, 1997. Pubmed reference: 9321385. DOI: 10.1093/emboj/16.20.6057.
Tagliavini, F., Mcarthur, R.A., Canciani, B., Giaccone, G., Porro, M., Bugiani, M., Lievens, P.M.J., Bugiani, O., Peri, E., Dallara, P., Rocchi, M., Poli, G., Forloni, G., Bandiera, T., Varasi, M., Suarato, A., Cassutti, P., Cervini, M.A., Lansen, J., Salmona, M., Post, C. :
Effectiveness of anthracycline against experimental prion disease in syrian hamsters Science 276:1119-1122, 1997. Pubmed reference: 9148807.
Vogel, G. :
Nobel prize - Prusiner recognized for once-heretical prion theory Science 278:214, 1997. Pubmed reference: 9340766.
Zhang, H., Stockel, J., Mehlhorn, I., Groth, D., Baldwin, M.A., Prusiner, S.B., James, T.L., Cohen, F.E. :
Physical studies of conformational plasticity in a recombinant prion protein Biochemistry 36:3543-3553, 1997. Pubmed reference: 9132005. DOI: 10.1021/bi961965r.
1996 Bamborough, P., Wille, H., Telling, G.C., Yehiely, F., Prusiner, S.B., Cohen, F.E. :
Prion protein structure and scrapie replication - theoretical, spectroscopic, and genetic investigations Cold Spring Harbor Symposia on Quantitative Biology 61:495-509, 1996. Pubmed reference: 9246476.
Beekes, M., Baldauf, E., Diringer, H. :
Sequential appearance and accumulation of pathognomonic markers in the central nervous system of hamsters orally infected with scrapie Journal of General Virology 77:1925-1934, 1996. Pubmed reference: 8760444.
Bountiff, L., Levantis, P., Oxford, J. :
Electrophoretic analysis of nucleic acids isolated from scrapie-infected hamster brain Journal of General Virology 77:2371-2378, 1996. Pubmed reference: 8811040.
Heller, J., Kolbert, A.C., Larsen, R., Ernst, M., Bekker, T., Baldwin, M., Prusiner, S.B., Pines, A., Wemmer, D.E. :
Solid-state nmr studies of the prion protein H1 fragment Protein Science 5:1655-1661, 1996. Pubmed reference: 8844854. DOI: 10.1002/pro.5560050819.
Kocisko, D.A., Lansbury, P.T., Caughey, B. :
Partial unfolding and refolding of scrapie-associated prion protein - evidence for a critical 16-KDA c-terminal domain Biochemistry 35:13434-13442, 1996. Pubmed reference: 8873612. DOI: 10.1021/bi9610562.
Mehlhorn, I., Groth, D., Stockel, J., Moffat, B., Reilly, D., Yansura, D., Willett, W.S., Baldwin, M., Fletterick, R., Cohen, F.E., Vandlen, R., Henner, D., Prusiner, S.B. :
High-level expression and characterization of a purified 142-RESIDUE polypeptide of the prion protein Biochemistry 35:5528-5537, 1996. Pubmed reference: 8611544. DOI: 10.1021/bi952965e.
Ovadia, H., Rosenmann, H., Shezen, E., Halimi, M., Ofran, I., Gabizon, R. :
Effect of scrapie infection on the activity of neuronal nitric-oxide synthase in brain and neuroblastoma cells Journal of Biological Chemistry 271:16856-16861, 1996. Pubmed reference: 8663207.
Prusiner, S.B. :
Molecular biology and genetics of prion diseases Cold Spring Harbor Symposia on Quantitative Biology 61:473-493, 1996. Pubmed reference: 9246475.
Taylor, D.M., Fernie, K. :
Exposure to autoclaving or sodium hydroxide extends the dose-response curve of the 263K strain of scrapie agent in hamsters Journal of General Virology 77:811-813, 1996. Pubmed reference: 8627270.
Ye, X., Carp, R.I. :
Histopathological changes in the pituitary glands of female hamsters infected with the 139H strain of scrapie Journal of Comparative Pathology 114:291-304, 1996. Pubmed reference: 8762587.
1995 Beekes, M., Baldauf, E., Cassens, S., Diringer, H., Keyes, P., Scott, A.C., Wells, G.A.H., Brown, P., Gibbs, C.J., Gajdusek, D.C. :
Western blot mapping of disease-specific amyloid in various animal species and humans with transmissible spongiform encephalopathies using a high-yield purification method Journal of General Virology 76:2567-2576, 1995. Pubmed reference: 7595360.
Bessen, R.A., Kocisko, D.A., Raymond, G.J., Nandan, S., Lansbury, P.T., Caughey, B. :
Non-genetic propagation of strain-specific properties of scrapie prion protein Nature 375:698-700, 1995. Pubmed reference: 7791905. DOI: 10.1038/375698a0.
Kocisko, D.A., Priola, S.A., Raymond, G.J., Chesebro, B., Lansbury, P.T., Caughey, B. :
Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier Proceedings of the National Academy of Sciences of the United States of America 92:3923-3927, 1995. Pubmed reference: 7732006.
Nguyen, J.T., Inouye, H., Baldwin, M.A., Fletterick, R.J., Cohen, F.E., Prusiner, S.B., Kirschner, D.A. :
X-ray diffraction of scrapie prion rods and PrP peptides Journal of Molecular Biology 252:412-422, 1995. Pubmed reference: 7563061. DOI: 10.1006/jmbi.1995.0507.
Priola, S.A., Chesebro, B. :
A single hamster prp amino acid blocks conversion to protease-resistant prp in scrapie-infected mouse neuroblastoma cells Journal of Virology 69:7754-7758, 1995. Pubmed reference: 7494285.
Race, R.E., Priola, S.A., Bessen, R.A., Ernst, D., Dockter, J., Rall, G.F., Mucke, L., Chesebro, B., Oldstone, M.B.A. :
Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent Neuron 15:1183-1191, 1995. Pubmed reference: 7576660.
1993 Borchelt, D.R., Rogers, M., Stahl, N., Telling, G., Prusiner, S.B. :
Release of the Cellular Prion Protein from Cultured Cells After Loss of Its Glycoinositol Phospholipid Anchor Glycobiology 3:319-329, 1993. Pubmed reference: 7691278.
Dearmond, S.J., Yang, S.L., Lee, A., Bowler, R., Taraboulos, A., Groth, D., Prusiner, S.B. :
3 Scrapie Prion Isolates Exhibit Different Accumulation Patterns of the Prion Protein Scrapie Isoform Proceedings of the National Academy of Sciences of the United States of America 90:6449-6453, 1993. Pubmed reference: 8101989.
1990 Lowenstein, D.H., Butler, D.A., Westaway, D., Mckinley, M.P., Dearmond, S.J., Prusiner, S.B. :
3 Hamster Species with Different Scrapie Incubation Times and Neuropathological Features Encode Distinct Prion Proteins Molecular and Cellular Biology 10:1153-1163, 1990. Pubmed reference: 2406562.

Edit History

  • Created by Frank Nicholas on 06 Sep 2005
  • Changed by Frank Nicholas on 15 May 2020
  • Changed by Imke Tammen2 on 23 Jan 2023
  • Changed by Imke Tammen2 on 23 Feb 2023