OMIA:000944-9541 : Spongiform encephalopathy, susceptibility/resistance to in Macaca fascicularis (crab-eating macaque)

In other species: Mallard , chicken , Ring-necked pheasant , white-tufted-ear marmoset , macaques , Rhesus monkey , dog , domestic ferret , domestic cat , puma , horse , pig , Arabian camel , deer , Eurasian elk , Western roe deer , red deer , Eastern wapiti , sika deer , Manchurian Wapiti , reindeer , black-tailed deer , white-tailed deer , American bison , taurine cattle , goat , mouflon , sheep , eland , greater kudu , gemsbok , rabbit , golden hamster , domestic guinea pig , domestic yak , chital , fallow deer , cheetah , raccoon dog , bighorn sheep , blue antelope , Arabian oryx , scimitar-horned oryx , nyala , Spanish ibex , water buffalo , Japanese quail , Pyrenean chamois , Iberian red deer , Bank vole , American mink

Categories: Nervous system phene

Links to possible relevant human trait(s) and/or gene(s) in OMIM: 176640 (gene) , 245300 (trait)

Links to relevant human diseases in MONDO:

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.

Species-specific description: Comoy et al. (2017) "present experimental evidence that transfusion in mice and non-human primates of blood products from symptomatic and non-symptomatic infected donors induces not only vCJD, but also a different class of neurological impairments. These impairments can all be retransmitted to mice with a pathognomonic accumulation of abnormal prion protein, thus expanding the spectrum of known prion diseases." Jaffré et al. (2023) "show that extensive analyses with current conventional techniques failed to detect any accumulation of abnormal prion protein (PrPv−CJD) in the CNS of these myelopathic animals [reported by Comoy et al. (2017)] ... . Conversely, in the spinal cord of these myelopathic primates, we observed an alteration of their physiological cellular PrP pattern: PrP was not detectable under its full-length classical expression but mainly under its physiological terminal-truncated C1 fragment. This observed disappearance of the N-terminal fragment of cellular PrP at the level of the lesions may provide the first experimental evidence of a link between loss of function of the cellular prion protein and disease onset."

Cite this entry

Nicholas, F. W., Tammen, I., & Sydney Informatics Hub. (2023). OMIA:000944-9541: Online Mendelian Inheritance in Animals (OMIA) [dataset].


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 Jaffré, N., Delmotte, J., Mikol, J., Deslys, J.P., Comoy, E. :
Unexpected decrease of full-length prion protein in macaques inoculated with prion-contaminated blood products. Front Mol Biosci 10:1164779, 2023. Pubmed reference: 37214335. DOI: 10.3389/fmolb.2023.1164779.
2021 Orge, L., Lima, C., Machado, C., Tavares, P., Mendonça, P., Carvalho, P., Silva, J., Pinto, M.L., Bastos, E., Pereira, J.C., Gonçalves-Anjo, N., Gama, A., Esteves, A., Alves, A., Matos, A.C., Seixas, F., Silva, F., Pires, I., Figueira, L., Vieira-Pinto, M., Sargo, R., Pires, M.D.A. :
Neuropathology of animal prion diseases. Biomolecules 11:466, 2021. Pubmed reference: 33801117. DOI: 10.3390/biom11030466.
2017 Comoy, E.E., Mikol, J., Jaffré, N., Lebon, V., Levavasseur, E., Streichenberger, N., Sumian, C., Perret-Liaudet, A., Eloit, M., Andreoletti, O., Haïk, S., Hantraye, P., Deslys, J.P. :
Experimental transfusion of variant CJD-infected blood reveals previously uncharacterised prion disorder in mice and macaque. Nat Commun 8:1268, 2017. Pubmed reference: 29097653. DOI: 10.1038/s41467-017-01347-0.
1996 Lasmezas, C.I., Deslys, J.P., Demaimay, R., Adjou, K.T., Lamoury, F., Dormont, D., Robain, O., Ironside, J., Hauw, J.J. :
BSE transmission to macaques Nature 381:743-744, 1996. Pubmed reference: 8657276. DOI: 10.1038/381743a0.

Edit History

  • Created by Frank Nicholas on 06 Sep 2005
  • Changed by Frank Nicholas on 15 May 2020
  • Changed by Imke Tammen2 on 24 May 2023
  • Changed by Imke Tammen2 on 16 Oct 2023