OMIA:000944-9901 : Spongiform encephalopathy, susceptibility/resistance to in Bison bison
In other species: domestic cat , taurine cattle , goat , pig , sheep , American mink , golden hamster , blue antelope , white-tufted-ear marmoset , eland , domestic ferret , greater kudu , Arabian oryx , mouflon , puma , Eastern wapiti , cheetah , chicken , crab-eating macaque , Rhesus monkey , macaques , black-tailed deer , rabbit , dog , water buffalo , Manchurian Wapiti , deer , domestic guinea pig , Iberian red deer , Western roe deer , fallow deer , Spanish ibex , Pyrenean chamois , horse , white-tailed deer , chital , Eurasian elk , nyala , gemsbok , scimitar-horned oryx , reindeer , Arabian camel , red deer , Mallard , sika deer , domestic yak , Ring-necked pheasant , raccoon dog , Bank vole , Japanese quail , bighorn sheep
Categories: Nervous system phene
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.
Cite this entry
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.
|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.|
|2003||Sigurdson, C.J., Miller, M.W. :|
|Other animal prion diseases. Br Med Bull 66:199-212, 2003. Pubmed reference: 14522860 . DOI: 10.1093/bmb/66.1.199.|
- Created by Imke Tammen2 on 21 Apr 2021