OMIA 000944-9031 : Spongiform encephalopathy in Gallus gallus

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 , crab-eating macaque , Rhesus monkey , macaques , black-tailed deer , , rabbit , dog , water buffalo , , Manchurian Wapiti , deer , domestic guinea pig , , Western roe deer , fallow deer , , , horse , white-tailed deer

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).

Associated gene:

Symbol Description Species Chr Location OMIA gene details page Other Links
Prnp prion protein Rattus norvegicus 3 NC_005102.4 (124515917..124531320) Prnp Homologene, Ensembl, NCBI gene


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.
2003 Matthews, D., Cooke, B.C. :
The potential for transmissible spongiform encephalopathies in non-ruminant livestock and fish Revue Scientifique et Technique 22:283-96, 2003. Pubmed reference: 12793786.
1999 Marcotte, E.M., Eisenberg, D. :
Chicken prion tandem repeats form a stable, protease-resistant domain Biochemistry 38:667-676, 1999. Pubmed reference: 9888807. DOI: 10.1021/bi981487f.
Wopfner, F., Weidenhofer, G., Schneider, R., von, Brunn, A., Gilch, S., Schwarz, T.F., Werner, T., Schatzl, M. :
Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein Journal of Molecular Biology 289:1163-1178, 1999. Pubmed reference: 10373359. DOI: 10.1006/jmbi.1999.2831.
1997 Cawthorne, R.J.G. :
Failure to confirm a TSE in chickens Veterinary Record 141:203, 1997. Pubmed reference: 9292978.
Narang, H. :
Failure to confirm a TSE in chickens Veterinary Record 141:255-256, 1997. Pubmed reference: 9308154.
1996 Pearce, F. :
BSE may lurk in pigs and chickens New Scientist 150:5, 1996.

Edit History

  • Created by Frank Nicholas on 06 Sep 2005
  • Changed by Frank Nicholas on 15 May 2020