OMIA 000944-9863 : Spongiform encephalopathy, susceptibility/resistance to in Cervus nippon

In other species: Mallard , chicken , white-tufted-ear marmoset , macaques , crab-eating macaque , Rhesus monkey , dog , domestic ferret , domestic cat , puma , horse , pig , Arabian camel , deer , Eurasian elk , Western roe deer , red deer , Eastern wapiti , Manchurian Wapiti , reindeer , black-tailed deer , white-tailed deer , American bison , cattle , goat , , sheep , eland , greater kudu , gemsbok , rabbit , golden hamster , domestic guinea pig , chital , fallow deer , cheetah , blue antelope , Arabian oryx , , scimitar-horned oryx , nyala , water buffalo , , , American mink ,

Possibly relevant human trait(s) and/or gene(s) (MIM number): 176640 (gene)

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.
2022 Roh, I.S., Kim, Y.C., Kim, H.J., Won, S.Y., Jeong, M.J., Hwang, J.Y., Kang, H.E., Sohn, H.J., Jeong, B.H. :
Polymorphisms of the prion-related protein gene are strongly associated with cervids' susceptibility to chronic wasting disease. Vet Rec 190:e940, 2022. Pubmed reference: 34562285. DOI: 10.1002/vetr.940.
Roh, I.S., Kim, Y.C., Won, S.Y., Jeong, M.J., Park, K.J., Park, H.C., Lee, Y.R., Kang, H.E., Sohn, H.J., Jeong, B.H. :
The first report of a strong association between genetic polymorphisms of the prion protein gene (PRNP) and susceptibility to chronic wasting disease (CWD) in sika deer (Cervus nippon). Transbound Emerg Dis :, 2022. Pubmed reference: 35349210. DOI: 10.1111/tbed.14543.
2021 Gallardo, M.J., Delgado, F.O. :
Animal prion diseases: A review of intraspecies transmission. Open Vet J 11:707-723, 2021. Pubmed reference: 35070868. DOI: 10.5455/OVJ.2021.v11.i4.23.

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  • Created by Imke Tammen2 on 27 Sep 2021