OMIA 000944-10141 : Spongiform encephalopathy in Cavia porcellus
In other species: domestic cat , cattle , goat , pig , sheep , American mink , golden hamster , blue antelope , white-tufted-ear marmoset , eland , domestic ferret , greater kudu , Arabian oryx , , puma , Eastern wapiti , cheetah , chicken , crab-eating macaque , Rhesus monkey , macaques , black-tailed deer , , rabbit , dog , water buffalo , , Manchurian Wapiti , deer , , Western roe deer , fallow deer , , , horse Possibly relevant human trait(s) and/or gene(s) (MIM number): 176640 Mendelian trait/disorder: unknown Considered a defect: unknown 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).
|2016||Watts, J.C., Giles, K., Saltzberg, D.J., Dugger, B.N., Patel, S., Oehler, A., Bhardwaj, S., Sali, A., Prusiner, S.B. :|
|Guinea Pig Prion Protein Supports Rapid Propagation of Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease Prions. J Virol 90:9558-9569, 2016. Pubmed reference: 27440899. DOI: 10.1128/JVI.01106-16.|
- Created by Frank Nicholas on 19 May 2017
- Changed by Frank Nicholas on 19 May 2017