OMIA 000944-447135 : Spongiform encephalopathy, susceptibility/resistance to in Myodes glareolus

In other species: Mallard , chicken , Ring-necked pheasant , 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 , sika deer , Manchurian Wapiti , reindeer , black-tailed deer , white-tailed deer , American bison , cattle , goat , , sheep , eland , greater kudu , gemsbok , rabbit , golden hamster , domestic guinea pig , domestic yak , chital , fallow deer , cheetah , raccoon dog , blue antelope , Arabian oryx , , scimitar-horned oryx , nyala , water buffalo , , , American mink ,

Category: 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: yes

Considered a defect: yes

Key variant known: yes

Year key variant first reported: 2022

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).

Species-specific description: Pirisinu et al. (2022): Nor98/atypical scrapie (AS) is a prion disease of sheep and goats ... . At variance with classical scrapie (CS), AS is considered poorly contagious and is supposed to be spontaneous in origin. The zoonotic potential of AS, its strain variability and the relationships with the more contagious CS strains remain largely unknown. We characterized AS isolates from sheep and goats by transmission ... in two genetic lines of bank voles, carrying either methionine (BvM) or isoleucine (BvI) at PrP residue 109. ... In bank voles, we found that the M109I polymorphism dictates the susceptibility to AS. BvI were susceptible and faithfully reproduced the AS strain, while the transmission in BvM was highly inefficient and was characterized by a conformational change towards a CS-like prion strain. Sub-passaging experiments revealed that the main strain component of AS is accompanied by minor CS-like strain components, which can be positively selected during replication in both AS-resistant or AS-susceptible animals."

Associated gene:

Symbol Description Species Chr Location OMIA gene details page Other Links
PRNP Myodes glareolus - no genomic information (-..-) PRNP Ensembl


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WARNING! Inclusion of a variant in this table does not automatically mean that it should be used for DNA testing. Anyone contemplating the use of any of these variants for DNA testing should examine critically the relevant evidence (especially in breeds other than the breed in which the variant was first described). If it is decided to proceed, the location and orientation of the variant sequence should be checked very carefully.

Since October 2021, OMIA includes a semiautomated lift-over pipeline to facilitate updates of genomic positions to a recent reference genome position. These changes to genomic positions are not always reflected in the ‘acknowledgements’ or ‘verbal description’ fields in this table.

OMIA Variant ID Breed(s) Variant Phenotype Gene Allele Type of Variant Source of Genetic Variant Reference Sequence Chr. g. or m. c. or n. p. Verbal Description EVA ID Inferred EVA rsID Year Published PubMed ID(s) Acknowledgements
1507 Susceptibility to atypical scrapie PRNP missense Naturally occurring variant p.(M109I) 2022 35731839


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 Bruno, R., Pirisinu, L., Riccardi, G., D'Agostino, C., De Cecco, E., Legname, G., Cardone, F., Gambetti, P., Nonno, R., Agrimi, U., Di Bari, M.A. :
Gerstmann-Sträussler-Scheinker disease with F198S mutation induces independent tau and prion protein pathologies in bank voles. Biomolecules 12:, 2022. Pubmed reference: 36291746. DOI: 10.3390/biom12101537.
Pirisinu, L., Di Bari, M.A., D'Agostino, C., Vanni, I., Riccardi, G., Marcon, S., Vaccari, G., Chiappini, B., Benestad, S.L., Agrimi, U., Nonno, R. :
A single amino acid residue in bank vole prion protein drives permissiveness to Nor98/atypical scrapie and the emergence of multiple strain variants. PLoS Pathog 18:e1010646, 2022. Pubmed reference: 35731839. DOI: 10.1371/journal.ppat.1010646.
2020 Nonno, R., Di Bari, M.A., Pirisinu, L., D'Agostino, C., Vanni, I., Chiappini, B., Marcon, S., Riccardi, G., Tran, L., Vikøren, T., Våge, J., Madslien, K., Mitchell, G., Telling, G.C., Benestad, S.L., Agrimi, U. :
Studies in bank voles reveal strain differences between chronic wasting disease prions from Norway and North America. Proc Natl Acad Sci U S A 117:31417-31426, 2020. Pubmed reference: 33229531. DOI: 10.1073/pnas.2013237117.
2016 Espinosa, J.C., Nonno, R., Di Bari, M., Aguilar-Calvo, P., Pirisinu, L., Fernández-Borges, N., Vanni, I., Vaccari, G., Marín-Moreno, A., Frassanito, P., Lorenzo, P., Agrimi, U., Torres, J.M. :
PrPC Governs Susceptibility to Prion Strains in Bank Vole, While Other Host Factors Modulate Strain Features. J Virol 90:10660-10669, 2016. Pubmed reference: 27654300. DOI: 10.1128/JVI.01592-16.
2008 Agrimi, U., Nonno, R., Dell'Omo, G., Di Bari, M.A., Conte, M., Chiappini, B., Esposito, E., Di Guardo, G., Windl, O., Vaccari, G., Lipp, H.P. :
Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles. PLoS Pathog 4:e1000113, 2008. Pubmed reference: 18654630. DOI: 10.1371/journal.ppat.1000113.
2006 Nonno, R., Di Bari, M.A., Cardone, F., Vaccari, G., Fazzi, P., Dell'Omo, G., Cartoni, C., Ingrosso, L., Boyle, A., Galeno, R., Sbriccoli, M., Lipp, H.P., Bruce, M., Pocchiari, M., Agrimi, U. :
Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles. PLoS Pathog 2:e12, 2006. Pubmed reference: 16518470. DOI: 10.1371/journal.ppat.0020012.

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  • Created by Imke Tammen2 on 15 Nov 2022
  • Changed by Imke Tammen2 on 15 Nov 2022
  • Changed by Imke Tammen2 on 24 Nov 2022