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Gene Review

PRNP  -  prion protein

Bos taurus

Synonyms: AltPrP, PrP
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Disease relevance of PRNP

  • Immunologic and molecular biologic studies of prion proteins in bovine spongiform encephalopathy [1].
  • Susceptibility to scrapie is largely controlled by the PRNP gene in mice and in several other species [2].
  • The appearance of a novel human prion disease, variant CJD, and the clear experimental evidence that it is caused by exposure to BSE has highlighted the need to understand the molecular basis of prion propagation, pathogenesis, and the barriers limiting intermammalian transmission [3].
  • We examined the ability of several recombinant antibody antigen-binding fragments (Fabs) to inhibit prion propagation in cultured mouse neuroblastoma cells (ScN2a) infected with PrPSc [4].
  • Prions cause a group of human and animal neurodegenerative diseases, which are now classified together because their etiology and pathogenesis, involve modification of the prion protein (PrP) [5].

Psychiatry related information on PRNP


High impact information on PRNP


Chemical compound and disease context of PRNP

  • The profile of microglial changes induced by the CJD agent differed substantially from activation induced by bacterial lipopolysaccharide or by beta-amyloid, a structure comparable to pathological PrP [11].
  • It is demonstrated here that a proline to leucine substitution in codon 168 of the ovine PrP protein gene is associated with increased resistance to experimental bovine spongiform encephalopathy (BSE) inoculation [12].
  • In this article, we describe for the first time the use of streptomycin sulfate in IHC, providing a novel original and easy way to amplify specifically PrPsc immunohistochemical detection in natural cases of BSE and scrapie, as well as in experimental TSEs in mice models using two different PrP antibodies [13].
  • The efficacy of three pretreatment techniques for the detection of prion protein (PrP) in formalin-fixed, paraffin-embedded bovine spongiform encephalopathy (BSE)--affected brain tissue were compared using automated image analysis [14].
  • The conserved bovine prion protein 121KHVAGAAAAGAVVGGLGGYMLGSAMSR147 transmembrane region (BPrP(tm)) contains a sequence rich in Gly residues [i.e., 130GAVVGGLGGYMLGSAMSR147 (BPrP(mi))] that shows homology with HIV-1 fusion peptide [15].

Biological context of PRNP


Anatomical context of PRNP

  • The level of nucleotide diversity in the complete bovine PRNP gene was pi = 0.00079, which is similar to that found at the bovine T-cell receptor alpha delta joining region (pi = 0.00077), but somewhat less than that observed for the bovine leptin (pi = 0.00265) [20].
  • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment [21].
  • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells [22].
  • Cellular prion protein expressed by bovine squamous epithelia of skin and upper gastrointestinal tract [23].
  • The presence of wild-type PrP molecules in the cytosol may have potential pathogenic implications [24].

Associations of PRNP with chemical compounds

  • Analysis of the gene encoding bovine PRNP revealed homozygosity for alleles encoding 6 octapeptide repeats, serine (S) at codon 46, and S at codon 146 in all samples [25].
  • Research over the past few years, however, demonstrates that the prion protein is a copper binding protein with high selectivity for Cu(2+) [26].
  • Cells incubated with N-acetyl-leucinal-leucinal-norleucinal (ALLN), lactacystin or MG132 accumulated both detergent-soluble and insoluble PrP species [24].
  • Short hairpin RNAs (shRNAs) were designed and screened for their ability to suppress the expression of caprine and bovine prion protein (PrP) [27].
  • Evaluation of quinacrine treatment for prion diseases [28].

Other interactions of PRNP


Analytical, diagnostic and therapeutic context of PRNP

  • Molecular cloning of the bovine PrP gene showed that it encodes a protein of 256 or 264 amino acids with five or six Gly:Pro-rich octarepeats, respectively, in contrast to all other mammalian PrP genes, which encode only five octarepeats [1].
  • Comparative sequence analysis and expression of bovine PrP gene in mouse L-929 cells [33].
  • The expression level of recombinant bovine PrP in the cells judged by immunofluorescence was higher than that of authentic mouse PrP [33].
  • In accordance with the lack of an interspecies barrier to BSE infection, we detected the typical signs of CNS spongiform degeneration by histopathological analysis and the presence of the bovine prion PrP(res) by Western blot or immunohistochemical analyses [34].
  • The recent discovery of significant associations between bovine spongiform encephalopathy (BSE) susceptibility in German cattle and the frequency distributions of insertion/deletion (indel) polymorphisms within the bovine PRNP gene prompted an evaluation of 132 commercial U.S. artificial insemination (AI) sires from 39 breeds [35].


  1. Immunologic and molecular biologic studies of prion proteins in bovine spongiform encephalopathy. Prusiner, S.B., Füzi, M., Scott, M., Serban, D., Serban, H., Taraboulos, A., Gabriel, J.M., Wells, G.A., Wilesmith, J.W., Bradley, R. J. Infect. Dis. (1993) [Pubmed]
  2. Detection of new quantitative trait Loci for susceptibility to transmissible spongiform encephalopathies in mice. Moreno, C.R., Lantier, F., Lantier, I., Sarradin, P., Elsen, J.M. Genetics (2003) [Pubmed]
  3. Prion diseases of humans and animals: their causes and molecular basis. Collinge, J. Annu. Rev. Neurosci. (2001) [Pubmed]
  4. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Peretz, D., Williamson, R.A., Kaneko, K., Vergara, J., Leclerc, E., Schmitt-Ulms, G., Mehlhorn, I.R., Legname, G., Wormald, M.R., Rudd, P.M., Dwek, R.A., Burton, D.R., Prusiner, S.B. Nature (2001) [Pubmed]
  5. Molecular biology and pathogenesis of prion diseases. Prusiner, S.B. Trends Biochem. Sci. (1996) [Pubmed]
  6. Dissociation of pathological and molecular phenotype of variant Creutzfeldt-Jakob disease in transgenic human prion protein 129 heterozygous mice. Asante, E.A., Linehan, J.M., Gowland, I., Joiner, S., Fox, K., Cooper, S., Osiguwa, O., Gorry, M., Welch, J., Houghton, R., Desbruslais, M., Brandner, S., Wadsworth, J.D., Collinge, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. Prion diseases and the BSE crisis. Prusiner, S.B. Science (1997) [Pubmed]
  8. Prion dementia without characteristic pathology. Collinge, J., Owen, F., Poulter, M., Leach, M., Crow, T.J., Rossor, M.N., Hardy, J., Mullan, M.J., Janota, I., Lantos, P.L. Lancet (1990) [Pubmed]
  9. Sequential targeting of the genes encoding immunoglobulin-mu and prion protein in cattle. Kuroiwa, Y., Kasinathan, P., Matsushita, H., Sathiyaselan, J., Sullivan, E.J., Kakitani, M., Tomizuka, K., Ishida, I., Robl, J.M. Nat. Genet. (2004) [Pubmed]
  10. PrP expression in B lymphocytes is not required for prion neuroinvasion. Klein, M.A., Frigg, R., Raeber, A.J., Flechsig, E., Hegyi, I., Zinkernagel, R.M., Weissmann, C., Aguzzi, A. Nat. Med. (1998) [Pubmed]
  11. Microglia from Creutzfeldt-Jakob disease-infected brains are infectious and show specific mRNA activation profiles. Baker, C.A., Martin, D., Manuelidis, L. J. Virol. (2002) [Pubmed]
  12. Ovine prion protein variant A136R154L168Q171 increases resistance to experimental challenge with bovine spongiform encephalopathy agent. Goldmann, W., Houston, F., Stewart, P., Perucchini, M., Foster, J., Hunter, N. J. Gen. Virol. (2006) [Pubmed]
  13. Amplified immunohistochemical detection of PrPsc in animal transmissible spongiform encephalopathies using streptomycin. Bencsik, A.A., Coleman, A.W., Debeer, S.O., Perron, H., Moussa, A. J. Histochem. Cytochem. (2006) [Pubmed]
  14. Hydrated autoclave pretreatment enhancement of prion protein immunoreactivity in formalin-fixed bovine spongiform encephalopathy-affected brain. Haritani, M., Spencer, Y.I., Wells, G.A. Acta Neuropathol. (1994) [Pubmed]
  15. The hydrophobic internal region of bovine prion protein shares structural and functional properties with HIV type 1 fusion peptide. Sáez-Cirión, A., Nieva, J.L., Gallaher, W.R. AIDS Res. Hum. Retroviruses (2003) [Pubmed]
  16. Frequencies of alleles and genotypes of the PRNP gene in Polish Red, Czech Pied and Czech Black-and-White cattle. Vrtková, I., Filistowicz, A., Dvorák, A., Wierzbicki, H., Szulc, T. J. Appl. Genet. (2001) [Pubmed]
  17. High incidence of single nucleotide polymorphisms in the prion protein gene of native Brazilian Caracu cattle. Kues, W.A., Ollhoff, R.D., Carnwath, J.W., de Souza, F.P., Madeira, H.M., Niemann, H. J. Anim. Breed. Genet. (2006) [Pubmed]
  18. Prion gene haplotypes of U.S. cattle. Clawson, M.L., Heaton, M.P., Keele, J.W., Smith, T.P., Harhay, G.P., Laegreid, W.W. BMC Genet. (2006) [Pubmed]
  19. Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. Rhie, A., Kirby, L., Sayer, N., Wellesley, R., Disterer, P., Sylvester, I., Gill, A., Hope, J., James, W., Tahiri-Alaoui, A. J. Biol. Chem. (2003) [Pubmed]
  20. Sequence variation in the bovine and ovine PRNP genes. Hills, D., Schlaepfer, J., Comincini, S., MacLean, I., Dolf, G., Ferretti, L., Olsaker, I., Williams, J.L. Anim. Genet. (2003) [Pubmed]
  21. Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Brown, D.R., Schmidt, B., Kretzschmar, H.A. Nature (1996) [Pubmed]
  22. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Rieger, R., Edenhofer, F., Lasmézas, C.I., Weiss, S. Nat. Med. (1997) [Pubmed]
  23. Cellular prion protein expressed by bovine squamous epithelia of skin and upper gastrointestinal tract. Pammer, J., Suchy, A., Rendl, M., Tschachler, E. Lancet (1999) [Pubmed]
  24. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. Yedidia, Y., Horonchik, L., Tzaban, S., Yanai, A., Taraboulos, A. EMBO J. (2001) [Pubmed]
  25. Experimental transmission of chronic wasting disease agent from mule deer to cattle by the intracerebral route. Hamir, A.N., Kunkle, R.A., Cutlip, R.C., Miller, J.M., O'Rourke, K.I., Williams, E.S., Miller, M.W., Stack, M.J., Chaplin, M.J., Richt, J.A. J. Vet. Diagn. Invest. (2005) [Pubmed]
  26. Copper binding in the prion protein. Millhauser, G.L. Acc. Chem. Res. (2004) [Pubmed]
  27. Suppression of prion protein in livestock by RNA interference. Golding, M.C., Long, C.R., Carmell, M.A., Hannon, G.J., Westhusin, M.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  28. Evaluation of quinacrine treatment for prion diseases. Barret, A., Tagliavini, F., Forloni, G., Bate, C., Salmona, M., Colombo, L., De Luigi, A., Limido, L., Suardi, S., Rossi, G., Auvré, F., Adjou, K.T., Salès, N., Williams, A., Lasmézas, C., Deslys, J.P. J. Virol. (2003) [Pubmed]
  29. Menstrum for culture preservation and medium for seed preparation in a tetanus toxin production process containing no animal or dairy products. Fang, A., Gerson, D.F., Demain, A.L. Lett. Appl. Microbiol. (2006) [Pubmed]
  30. Clusterin in bovine spongiform encephalopathy (BSE). McHattie, S., Wells, G.A., Bee, J., Edington, N. J. Comp. Pathol. (1999) [Pubmed]
  31. Hypothesis: the meeting place model for prion disease. Norris, V., Cellier, D., Caston, J., Valleton, J.M., Sweetman, G., Monnier, C. C. R. Acad. Sci. III, Sci. Vie (1997) [Pubmed]
  32. Development and validation of a bovine macrophage specific cDNA microarray. Jensen, K., Talbot, R., Paxton, E., Waddington, D., Glass, E.J. BMC Genomics (2006) [Pubmed]
  33. Comparative sequence analysis and expression of bovine PrP gene in mouse L-929 cells. Yoshimoto, J., Iinuma, T., Ishiguro, N., Horiuchi, M., Imamura, M., Shinagawa, M. Virus Genes (1992) [Pubmed]
  34. Different behavior toward bovine spongiform encephalopathy infection of bovine prion protein transgenic mice with one extra repeat octapeptide insert mutation. Castilla, J., Gutiérrez-Adán, A., Brun, A., Pintado, B., Parra, B., Ramírez, M.A., Salguero, F.J., Díaz San Segundo, F., Rábano, A., Cano, M.J., Torres, J.M. J. Neurosci. (2004) [Pubmed]
  35. Comparative PRNP genotyping of U.S. cattle sires for potential association with BSE. Seabury, C.M., Womack, J.E., Piedrahita, J., Derr, J.N. Mamm. Genome (2004) [Pubmed]
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