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Gene Review

PRPC  -  prion protein

Ovis aries

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Disease relevance of PRPC


Psychiatry related information on PRPC

  • BACKGROUND: In sheep, susceptibility to scrapie, which is similar to human prion diseases such as Kuru and variant Creutzfeldt-Jakob disease (vCJD), is determined by prion protein (PrP) gene (Prnp) polymorphisms [6].
  • Furthermore, in vitro conversion reactions with different prion strains revealed that the degree of alteration of the conversion efficiency induced by amino acid exchanges was varying according to the prion strain [7].
  • TSEs are usually rapidly progressive and clinical symptoms comprise dementia and loss of movement coordination due to the accumulation of an abnormal isoform (PrP(Sc)) of the host-encoded prion protein (PrP(c)) [8].
  • In an immunohistochemical study of naturally-occurring and experimental scrapie in sheep, deposits of cerebrovascular amyloid were found to react with antibodies to hamster scrapie prion protein (PrP 27-30), but not with antibodies to the amyloid beta-protein of Alzheimer's disease [9].
  • These findings indicate that cell biological properties of ovine PrP can vary with natural polymorphisms and raise the possibility that differential interactions of PrP variants with the cellular machinery may contribute to permissiveness or resistance to prion multiplication [10].

High impact information on PRPC


Chemical compound and disease context of PRPC

  • The cellular prion protein (PrPC), a membrane glycoprotein anchored to the outer surface of neurons, lymphocytes and other cells, is associated directly with the pathogenesis of the transmissible spongiform encephalopathies (TSEs) occurring mainly in humans, cattle, sheep and goats [15].
  • We isolated blood samples from 222 sheep representing the eight main local sheep breeds in the Xinjiang Autonomous Region, the territory with the most abundant local sheep breeds in China, to identify the PRNP polymorphisms and to determine whether these breeds were at risk for developing scrapie [1].
  • We have cured the scrapie-infected, clonal SMB cell line with pentosan sulfate, stably re-infected it with a different strain of scrapie and shown that biological properties and prion protein profiles characteristic of each original strain are propagated faithfully in this single non-neuronal cell type [16].
  • Scrapie in the U.S. Suffolk breed and in many breeds in Europe occurs in sheep homozygous for glutamine (171QQ), but rarely in sheep heterozygous for glutamine and arginine (171QR) or homozygous for arginine (171RR) at codon 171 of the PrP gene [17].
  • To further identify the critical molecular components of the CJD agent, 120S infectious material with reduced prion protein (PrP) was treated with guanidine hydrochloride or SDS [18].

Biological context of PRPC


Anatomical context of PRPC


Associations of PRPC with chemical compounds

  • The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH [26].
  • A new PRNP polymorphism encoding either glycine (G) or arginine (R) at codon 85 as well as eight previously reported polymorphisms at codons 101, 112, 127, 141, 146, 154, 171, and 189 in other sheep breeds were detected [1].
  • Probing the dynamics of prion diseases with amphotericin B [27].
  • Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction [28].
  • Prion diseases: what is the neurotoxic molecule [29]?

Regulatory relationships of PRPC

  • Polymorphisms of the prion protein gene PRNP have been shown to influence the susceptibility/resistance to prion infections in human and sheep [30].

Other interactions of PRPC

  • Various data indicate that the polymorphisms within the open reading frame (ORF) of PrP are associated with the susceptibility and control the species barrier in prion diseases [31].
  • Eyes, optic nerves and brain from each animal were fixed and histologically processed using hematoxylin-eosin, followed by immunohistochemical staining for prion protein (PrPsc) and glial fibrillar acidic protein (GFAP) [32].
  • In this report, we describe targeted deletion at the GGTA1 (alpha 1,3-galactosyl transferase) and PrP (prion protein) loci in primary fibroblasts from livestock [33].

Analytical, diagnostic and therapeutic context of PRPC

  • Genotyping of ovine prion protein gene (PRNP) variants by PCR with melting curve analysis [34].
  • Extracellular collections of abnormal filaments composed of prion proteins have been identified in the brains of scrapie-infected hamsters using immunoelectron microscopy [12].
  • To clarify the separate roles of FDCs and lymphocytes, we produced chimeric mice with a mismatch in PrP status between FDCs and other cells of the immune system, by grafting bone marrow from PrP-deficient knockout mice into PrP-expressing mice and vice versa [14].
  • Upon exposure to low doses of infectious agent, such cultures, unlike cultures originating from PrP null mice, were found to accumulate de novo abnormal PrP and infectivity, as assessed by mouse bioassay [35].
  • Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures [36].


  1. Prion protein gene (PRNP) polymorphisms in Xinjiang local sheep breeds in China. Lan, Z., Wang, Z.L., Liu, Y., Zhang, X. Arch. Virol. (2006) [Pubmed]
  2. Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep. Andréoletti, O., Morel, N., Lacroux, C., Rouillon, V., Barc, C., Tabouret, G., Sarradin, P., Berthon, P., Bernardet, P., Mathey, J., Lugan, S., Costes, P., Corbière, F., Espinosa, J.C., Torres, J.M., Grassi, J., Schelcher, F., Lantier, F. J. Gen. Virol. (2006) [Pubmed]
  3. Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion. Rigter, A., Bossers, A. J. Gen. Virol. (2005) [Pubmed]
  4. Molecular evolution of the sheep prion protein gene. Slate, J. Proc. Biol. Sci. (2005) [Pubmed]
  5. Somatic cell mapping of the bovine prion protein gene and restriction fragment length polymorphism studies in cattle and sheep. Ryan, A.M., Womack, J.E. Anim. Genet. (1993) [Pubmed]
  6. Resistance to scrapie in PrP ARR/ARQ heterozygous sheep is not caused by preferential allelic use. Caplazi, P.A., O'Rourke, K.I., Baszler, T.V. J. Clin. Pathol. (2004) [Pubmed]
  7. Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo. Piening, N., Nonno, R., Di Bari, M., Walter, S., Windl, O., Agrimi, U., Kretzschmar, H.A., Bertsch, U. J. Biol. Chem. (2006) [Pubmed]
  8. Novel Aspects of Prions, Their Receptor Molecules, and Innovative Approaches for TSE Therapy. Vana, K., Zuber, C., Nikles, D., Weiss, S. Cell. Mol. Neurobiol. (2007) [Pubmed]
  9. Cerebrovascular amyloid in scrapie-affected sheep reacts with antibodies to prion protein. Allsop, D., Ikeda, S., Bruce, M., Glenner, G.G. Neurosci. Lett. (1988) [Pubmed]
  10. Prion proteins from susceptible and resistant sheep exhibit some distinct cell biological features. Sabuncu, E., Paquet, S., Chapuis, J., Moudjou, M., Lai, T.L., Grassi, J., Baron, U., Laude, H., Vilette, D. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Westaway, D., DeArmond, S.J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S.L., Torchia, M., Carlson, G.A., Prusiner, S.B. Cell (1994) [Pubmed]
  12. Identification of prion amyloid filaments in scrapie-infected brain. DeArmond, S.J., McKinley, M.P., Barry, R.A., Braunfeld, M.B., McColloch, J.R., Prusiner, S.B. Cell (1985) [Pubmed]
  13. PrPSc accumulation in myocytes from sheep incubating natural scrapie. Andréoletti, O., Simon, S., Lacroux, C., Morel, N., Tabouret, G., Chabert, A., Lugan, S., Corbière, F., Ferré, P., Foucras, G., Laude, H., Eychenne, F., Grassi, J., Schelcher, F. Nat. Med. (2004) [Pubmed]
  14. Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells. Brown, K.L., Stewart, K., Ritchie, D.L., Mabbott, N.A., Williams, A., Fraser, H., Morrison, W.I., Bruce, M.E. Nat. Med. (1999) [Pubmed]
  15. Functional disruption of the prion protein gene in cloned goats. Yu, G., Chen, J., Yu, H., Liu, S., Chen, J., Xu, X., Sha, H., Zhang, X., Wu, G., Xu, S., Cheng, G. J. Gen. Virol. (2006) [Pubmed]
  16. Scrapie strains maintain biological phenotypes on propagation in a cell line in culture. Birkett, C.R., Hennion, R.M., Bembridge, D.A., Clarke, M.C., Chree, A., Bruce, M.E., Bostock, C.J. EMBO J. (2001) [Pubmed]
  17. Pregnancy status and fetal prion genetics determine PrPSc accumulation in placentomes of scrapie-infected sheep. Tuo, W., O'Rourke, K.I., Zhuang, D., Cheevers, W.P., Spraker, T.R., Knowles, D.P. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  18. Viral particles are required for infection in neurodegenerative Creutzfeldt-Jakob disease. Manuelidis, L., Sklaviadis, T., Akowitz, A., Fritch, W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  19. Linkage disequilibrium across six prion gene regions spanning 20 kbp in U.S. sheep. Green, B.T., Heaton, M.P., Clawson, M.L., Laegreid, W.W. Mamm. Genome (2006) [Pubmed]
  20. Evaluation of associations between prion haplotypes and growth, carcass, and meat quality traits in a Dorset x Romanov sheep population. Isler, B.J., Freking, B.A., Thallman, R.M., Heaton, M.P., Leymaster, K.A. J. Anim. Sci. (2006) [Pubmed]
  21. Susceptibility of transgenic mice expressing chimeric sheep, bovine and human PrP genes to sheep scrapie. Gombojav, A., Shimauchi, I., Horiuchi, M., Ishiguro, N., Shinagawa, M., Kitamoto, T., Miyoshi, I., Mohri, S., Takata, M. J. Vet. Med. Sci. (2003) [Pubmed]
  22. The incidence of genotypes at codon 171 of the prion protein gene (PRNP) in five breeds of sheep and production traits of ewes associated with those genotypes. Alexander, B.M., Stobart, R.H., Russell, W.C., O'Rourke, K.I., Lewis, G.S., Logan, J.R., Duncan, J.V., Moss, G.E. J. Anim. Sci. (2005) [Pubmed]
  23. Compartmentalization of prion isoforms within the reproductive tract of the ram. Ecroyd, H., Sarradin, P., Dacheux, J.L., Gatti, J.L. Biol. Reprod. (2004) [Pubmed]
  24. Japanese scrapie cases. Onodera, T., Saeki, K. Jpn. J. Infect. Dis. (2000) [Pubmed]
  25. Neurotoxicity of a prion protein fragment. Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F. Nature (1993) [Pubmed]
  26. The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH. Granata, V., Palladino, P., Tizzano, B., Negro, A., Berisio, R., Zagari, A. Biopolymers (2006) [Pubmed]
  27. Probing the dynamics of prion diseases with amphotericin B. Adjou, K.T., Deslys, J.P., Demaimay, R., Dormont, D. Trends Microbiol. (1997) [Pubmed]
  28. Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction. Blanch, E.W., Gill, A.C., Rhie, A.G., Hope, J., Hecht, L., Nielsen, K., Barron, L.D. J. Mol. Biol. (2004) [Pubmed]
  29. Prion diseases: what is the neurotoxic molecule? Chiesa, R., Harris, D.A. Neurobiol. Dis. (2001) [Pubmed]
  30. DNA polymorphisms of the prion doppel gene region in four different German cattle breeds and cows tested positive for bovine spongiform encephalopathy. Balbus, N., Humeny, A., Kashkevich, K., Henz, I., Fischer, C., Becker, C.M., Schiebel, K. Mamm. Genome (2005) [Pubmed]
  31. Amino acid sequence of the Amur tiger prion protein. Wu, C., Pang, W., Zhao, D. Virus Res. (2006) [Pubmed]
  32. Pathological findings in retina and visual pathways associated to natural Scrapie in sheep. Hortells, P., Monzón, M., Monleón, E., Acín, C., Vargas, A., Bolea, R., Luján, L., Badiola, J.J. Brain Res. (2006) [Pubmed]
  33. Gene targeting in primary fetal fibroblasts from sheep and pig. Denning, C., Dickinson, P., Burl, S., Wylie, D., Fletcher, J., Clark, A.J. Cloning Stem Cells (2001) [Pubmed]
  34. Genotyping of ovine prion protein gene (PRNP) variants by PCR with melting curve analysis. Schütz, E., Scharfenstein, M., Brenig, B. Clin. Chem. (2006) [Pubmed]
  35. Prions can infect primary cultured neurons and astrocytes and promote neuronal cell death. Cronier, S., Laude, H., Peyrin, J.M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  36. Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures. Arjona, A., Simarro, L., Islinger, F., Nishida, N., Manuelidis, L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
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