OMIA 000944-9615 : Spongiform encephalopathy in Canis lupus familiaris

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 , 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).

References


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.
2020 Kim, D.J., Kim, Y.C., Kim, A.D., Jeong, B.H. :
Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (<i>PRNP</i>) in Dogs-A Resistant Animal of Prion Disease. Int J Mol Sci 21:, 2020. Pubmed reference: 32532135. DOI: 10.3390/ijms21114160.
Zhang, J. :
Molecular Dynamics Studies of Dog Prion Protein Wild-type and Its D159N Mutant. J Biomol Struct Dyn :1-12, 2020. Pubmed reference: 32496928. DOI: 10.1080/07391102.2020.1776155.
2018 Sanchez-Garcia, J., Fernandez-Funez, P. :
D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals. Neurobiol Dis 119:1-12, 2018. Pubmed reference: 30010001. DOI: 10.1016/j.nbd.2018.07.011.
2012 Stewart, P., Campbell, L., Skogtvedt, S., Griffin, K.A., Arnemo, J.M., Tryland, M., Girling, S., Miller, M.W., Tranulis, M.A., Goldmann, W. :
Genetic predictions of prion disease susceptibility in carnivore species based on variability of the prion gene coding region. PLoS One 7:e50623, 2012. Pubmed reference: 23236380. DOI: 10.1371/journal.pone.0050623.
2003 Nitzan-Kaluski, D., Leventhal, A. :
Bovine spongiform encephalopathy in Israel: implications for human health Israel Medical Association Journal: Imaj 5:662-5, 2003.
2002 De Bosschere, H., Bos, M., Ducatelle, R., Bhatti, S., Van Ham, L. :
Spongiform degeneration of the white matter in the central nervous system of Australian cattle dog littermates Vlaams Diergeneeskundig Tijdschrift 71:145-148, 2002.

Edit History


  • Created by Frank Nicholas on 06 Sep 2005
  • Changed by Tosso Leeb on 03 Dec 2015
  • Changed by Frank Nicholas on 15 May 2020