OMIA 000944-89462 : Spongiform encephalopathy in Bubalus bubalis

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 , , Manchurian Wapiti , deer , domestic guinea pig , , 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: 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).

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.
2016 Yaman, Y., Karadağ, O., Ün, C. :
Investigation of the prion protein gene (PRNP) polymorphisms in Anatolian, Murrah, and crossbred water buffaloes (Bubalus bubalis). Trop Anim Health Prod :, 2016. Pubmed reference: 27822596. DOI: 10.1007/s11250-016-1185-4.
2015 Zhao, H., Du, Y., Chen, S., Qing, L., Wang, X., Huang, J., Wu, D., Zhang, Y. :
The prion protein gene polymorphisms associated with bovine spongiform encephalopathy susceptibility differ significantly between cattle and buffalo. Infect Genet Evol 36:531-8, 2015. Pubmed reference: 26319996. DOI: 10.1016/j.meegid.2015.08.031.
2012 Imran, M., Mahmood, S., Babar, M.E., Hussain, R., Yousaf, M.Z., Abid, N.B., Lone, K.P. :
PRNP gene variation in Pakistani cattle and buffaloes. Gene 505:180-5, 2012. Pubmed reference: 22634099. DOI: 10.1016/j.gene.2012.05.038.
1998 Iannuzzi, L., Palomba, R., Dimeo, G.P., Perucatti, A., Ferrara, L. :
Comparative FISH-mapping of the prion protein gene (PrnP) on cattle, river buffalo, sheep and goat chromosomes Cytogenetics & Cell Genetics 81:202-204, 1998.

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  • Created by Frank Nicholas on 06 Sep 2005