OMIA:000944-9863 : Spongiform encephalopathy, susceptibility/resistance to in Cervus nippon
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 , domestic guinea pig , , Western roe deer , fallow deer , , , horse , white-tailed deer , chital , American bison , Eurasian elk , nyala , gemsbok , scimitar-horned oryx , reindeer , Arabian camel , red deer , Mallard , domestic yak , Ring-necked pheasant , raccoon dog , Bank vole , Japanese quail
Categories: Nervous system phene
Possibly relevant human trait(s) and/or gene(s) (MIM number): 176640 (gene)
Links to MONDO diseases: No links.
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). In ruminants the disease has been called bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep and goats and chronic wasting disease (CWD) in cervids.
Molecular basis: Roh et al. (2022) "investigated genetic polymorphisms of the PRNP gene using amplicon sequencing in sika deer. In addition, to identify a genetic susceptibility factor, we compared the genotype, allele and haplotype frequencies of the PRNP gene between CWD-positive and CWD-negative sika deer. Furthermore, to assess the effect of the genetic polymorphisms on sika deer prion protein (PrP), we performed in silico analysis using PolyPhen-2, PROVEAN and AMYCO. Finally, we analysed the tertiary structure and electrostatic potential of sika deer PrP based on single nucleotide polymorphisms (SNPs) using the SWISS-MODEL and Swiss-PdbViewer programs. We found a total of 24 SNPs of the PRNP gene, including 22 novel SNPs (10 synonymous SNPs and 12 nonsynonymous SNPs), in sika deer. Among the nonsynonymous SNPs, we found a strong association of susceptibility to CWD with c.56G > A (Ser19Asn). In addition, we found that c.56G > A (Ser19Asn), c.296A > T (His99Leu) and c.560T > A (Val187Asp) were predicted to have damaging effects on sika deer PrP. Furthermore, we observed significant alterations in the electrostatic potential of sika deer PrP by genetic polymorphisms of the 187Asp allele."
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.
|2023||Tranulis, M.A., Tryland, M. :|
|The zoonotic potential of chronic wasting disease - A review. Foods 12:824, 2023. Pubmed reference: 36832899 . DOI: 10.3390/foods12040824.|
|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. :|
|First report of a strong association between genetic polymorphisms of the prion protein gene (PRNP) and susceptibility to chronic wasting disease in sika deer (Cervus nippon). Transbound Emerg Dis 69:e2073-e2083, 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.|
- Created by Imke Tammen2 on 27 Sep 2021
- Changed by Imke Tammen2 on 25 Nov 2022