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Prion diseases and genetic susceptibility

Year 2025, Volume: 9 Issue: 1, 65 - 74, 30.04.2025

Canan Güven , Iraz Akış Akad

Abstract

Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are fatal neurodegenerative disorders caused by misfolding of the prion protein (PrP). These diseases affect both humans and animals, leading to severe neurological deterioration. Prion diseases in humans include Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI), and kuru. Known forms in animals include Scrapie, Bovine Spongiform Encephalopathy (BSE), Chronic Wasting Disease (CWD), Transmissible Mink Encephalopathy (TME) and Feline Spongiform Encephalopathy (FSE). One of the key factors affecting susceptibility to prion disease is genetic variation in the PRNP gene, which encodes PrP. Among the most studied polymorphisms, the M129V variant in humans plays a major role in disease susceptibility. Homozygosity for methionine (M/M) at codon 129 increases the risk of prion diseases, while heterozygosity (M/V) provides partial resistance. Similarly, in animals, specific PRNP polymorphisms such as Q171R in sheep confer resistance to scrapie, while certain genetic variants in deer affect CWD susceptibility. These polymorphisms are important for understanding disease transmission, species barriers, and potential resistance mechanisms. This review comprehensively examines prion diseases in both humans and animals, focusing on PRNP polymorphisms and their effects on disease susceptibility. Understanding these genetic variations is important for disease prevention, risk assessment, and development of potential treatment strategies.

Keywords

prion diseases PRNP polymorphisms transmissible spongiform encephalopathies genetic susceptibility.

References

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  • Baldwin, K. J., & Correll, C. M. (2019). Prion Disease. Seminars in Neurology, 39(04), 428–439.
  • Bossers, A., Belt, P. B. G. M., Raymond, G. J., Caughey, B., de Vries, R., & Smits, M. A. (1997). Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms. Proceedings of the National Academy of Sciences of the United States of America, 94(10), 4931-4936.
  • Bradley, R. (2002). Bovine spongiform encephalopathy: Update. Acta Neurobiologiae Experimentalis (Wars), 62(3), 183-195.
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  • Chesebro, B. (2003). Introduction to the transmissible spongiform encephalopathies or prion diseases. British Medical Bulletin, 66(1), 1–20.
  • Dearmond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., & Prusinert, S. B. (1985). Identification of prion amyloid filaments in Scrapie-infected brain. Cell, 41(1), 221–235.
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  • Gallardo M.J., & Delgado F.O., 2021, Animal prion diseases: A review of intraspecies transmission. Open Veterinary Journals, 11(4), 707–723.
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  • Gurgul, A., & Slota, E. (2007). Effect of bovine PRNP gene polymorphisms on BSE susceptibility in cattle. Folia Biologica (Kraków), 55(3-4), 81–86.
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  • Hizume, M., & Mizusawa, H. (2007). [Establishment of the concept of prion diseases]. Nihon Rinsho, 65(8), 1373-1378.
  • Houston, F., & Andréoletti, O. (2019). Animal prion diseases: the risks to human health. Brain Pathology, 29(2), 248–262.
  • Hunter, N. (1998). Scrapie. Molecular Biotechnology, 9(3), 225–234.
  • Hwang, S., & Nicholson, E. M. (2018). Thermodynamic characterization for the denatured state of bovine prion protein and the BSE associated variant E211K. Prion, 12(5-6), 301-309.
  • Iwasaki, Y. (2016). Creutzfeldt-Jakob disease, Neuropathology, 37(2), 174–188.
  • Jacobs, J. G., Bossers, A., Rezaei, H., van Keulen, L. J. M., McCutcheon, S., Sklaviadis, T., Lantier, I., Berthon, P., Lantier, F., van Zijderveld, F. G., & Langeveld, J. P. M. (2011). Proteinase K-resistant material in ARR/VRQ sheep brain affected with classical scrapie is composed mainly of VRQ prion protein. Journal of Virology, 85(23), 12537-12546.
  • Jewell, J. E. (2005). Low frequency of PrP genotype 225SF among free-ranging mule deer (Odocoileus hemionus) with chronic wasting disease. Journal of General Virology, 86(8), 2127–2134.
  • Johnson, C. (2006). Prion protein polymorphisms in white-tailed deer influence susceptibility to chronic wasting disease. Journal of General Virology, 87(7), 2109–2114.
  • Khan, Z., Sankari, A., & Bollu, P.C. (2024) Fatal familial insomnia, StatPearls Publishing, Treasure Island (FL).
  • Kim, Y.-C., & Jeong, B.-H. (2021). The First Meta-Analysis of the M129V Single-Nucleotide Polymorphism (SNP) of the Prion Protein Gene (PRNP) with Sporadic Creutzfeldt-Jakob Disease. Cells, 10(11), 3132.
  • Kim, D. J., Kim, Y. C., Kim, A. D., & Jeong, B. H. (2020). Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (PRNP) in Dogs—A Resistant Animal of Prion Disease. International Journal of Molecular Sciences, 21(11), 4160.
  • Kim, H.H., Kim, Y.C., Kim, K., Kim, A. D., Jeong, B., H. (2021). Novel Polymorphisms and Genetic Features of the Prion Protein Gene (PRNP) in Cats, Hosts of Feline Spongiform Encephalopathy. Genes, 24;12(1):13.
  • Kimberlin, R. H. (1992). Bovine spongiform encephalopathy. Rev Sci Tech, 11(2), 347-489.
  • Kobayashi, A., Teruya, K., Matsuura, Y., Shirai, T., Nakamura, Y., Yamada, M., Mizusawa, H., Mohri, S., & Kitamoto, T. (2015). The influence of PRNP polymorphisms on human prion disease susceptibility: an update. Acta Neuropathologica, 130(2), 159-170.
  • Konold, T., Spiropoulos, J., Chaplin, M. J., Thorne, L., Spencer, Y. I., Wells, G. A. H., & Hawkins, S. A. C. (2009). Transmissibility studies of vacuolar changes in the rostral colliculus of pigs. BMC Veterinary Research, 5(35), 1-13.
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Prion diseases and genetic susceptibility

Year 2025, Volume: 9 Issue: 1, 65 - 74, 30.04.2025

Canan Güven , Iraz Akış Akad

Abstract

Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are fatal neurodegenerative disorders caused by misfolding of the prion protein (PrP). These diseases affect both humans and animals, leading to severe neurological deterioration. Prion diseases in humans include Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI), and kuru. Known forms in animals include Scrapie, Bovine Spongiform Encephalopathy (BSE), Chronic Wasting Disease (CWD), Transmissible Mink Encephalopathy (TME) and Feline Spongiform Encephalopathy (FSE). One of the key factors affecting susceptibility to prion disease is genetic variation in the PRNP gene, which encodes PrP. Among the most studied polymorphisms, the M129V variant in humans plays a major role in disease susceptibility. Homozygosity for methionine (M/M) at codon 129 increases the risk of prion diseases, while heterozygosity (M/V) provides partial resistance. Similarly, in animals, specific PRNP polymorphisms such as Q171R in sheep confer resistance to scrapie, while certain genetic variants in deer affect CWD susceptibility. These polymorphisms are important for understanding disease transmission, species barriers, and potential resistance mechanisms. This review comprehensively examines prion diseases in both humans and animals, focusing on PRNP polymorphisms and their effects on disease susceptibility. Understanding these genetic variations is important for disease prevention, risk assessment, and development of potential treatment strategies.

Keywords

prion diseases PRNP polymorphisms transmissible spongiform encephalopathies genetic susceptibility.

References

  • Angers, R., Christiansen, J., Nalls, A. V., Kang, H.-E., Hunter, N., Hoover, E., Mathiason, C. K., Sheetz, M., & Telling, G. C. (2014). Structural effects of PrP polymorphisms on intra- and interspecies prion transmission. Proceedings of the National Academy of Sciences, 111(30), 11169-11174.
  • Asher, D. M., & Gregori, L. (2018). Human transmissible spongiform encephalopathies: Historic view. Handbook of Clinical Neurology, 1–17.
  • Baldwin, K. J., & Correll, C. M. (2019). Prion Disease. Seminars in Neurology, 39(04), 428–439.
  • Bossers, A., Belt, P. B. G. M., Raymond, G. J., Caughey, B., de Vries, R., & Smits, M. A. (1997). Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms. Proceedings of the National Academy of Sciences of the United States of America, 94(10), 4931-4936.
  • Bradley, R. (2002). Bovine spongiform encephalopathy: Update. Acta Neurobiologiae Experimentalis (Wars), 62(3), 183-195.
  • Brandel, J.-P., & Knight, R. (2018). Variant Creutzfeldt–Jakob disease. Handbook of Clinical Neurology, 191–205.
  • Bruce, M. E., Will, R. G., Ironside, J. W., McConnell, I., Drummond, D., Suttie, A., McCardle, L., Chree, A., Hope, J., Birkett, C., Cousens, S., Fraser, H., Bostock, C. J. (1997). Transmissions to mice indicate that “new variant” CJD is caused by the BSE agent. Nature, 389(6650), 498–501.
  • Cassmann, E. D., & Greenlee, J. J. (2020). Pathogenesis, detection, and control of scrapie in sheep. American Journal of Veterinary Research, 81(7), 600–614.
  • Chesebro, B. (2003). Introduction to the transmissible spongiform encephalopathies or prion diseases. British Medical Bulletin, 66(1), 1–20.
  • Dearmond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., & Prusinert, S. B. (1985). Identification of prion amyloid filaments in Scrapie-infected brain. Cell, 41(1), 221–235.
  • Erdtmann, R., & Sivitz, L. (Eds.)., 2003, Advancing prion science: Guidance for the National Prion Research Program: Interim report. Institute of Medicine, Committee on Transmissible Spongiform Encephalopathies. National Academies Press.
  • Gallardo M.J., & Delgado F.O., 2021, Animal prion diseases: A review of intraspecies transmission. Open Veterinary Journals, 11(4), 707–723.
  • Gidalevitz, T., Wang, N., Deravaj, T., Alexander-Floyd, J., & Morimoto, R. I. (2013). Natural genetic variation determines susceptibility to aggregation or toxicity in a C. elegans model for polyglutamine disease. BMC Biology, 11, Article 100.
  • Goldmann, W. (2018). Classic and atypical scrapie: A genetic perspective. In Handbook of clinical neurology, 111-120.
  • Gupta, P. K. (1997). 1997 Nobel Prize for Medicine: Prions as proteinaceous infectious particles. Current Science, 73(12), 1041-1045.
  • Gurgul, A., & Slota, E. (2007). Effect of bovine PRNP gene polymorphisms on BSE susceptibility in cattle. Folia Biologica (Kraków), 55(3-4), 81–86.
  • Haase, B., Doherr, M. G., Seuberlich, T., Drögemüller, C., Dolf, G., Nicken, P., Schiebel, K., Ziegler, U., Groschup, M. H., Zurbriggen, A., & Leeb, T. (2007). PRNP promoter polymorphisms are associated with BSE susceptibility in Swiss and German cattle. BMC Genetics, 8(15), 1-8.
  • Heaton, M. P., Keele, J. W., Harhay, G. P., Richt, J. A., Koohmaraie, M., Wheeler, T. L., Shackelford, S. D., Casas, E., King, D. A., Sonstegard, T. S., Van Tassell, C. P., Neibergs, H. L., Chase, C. C., Kalbfleisch, T. S., Smith, T. P. L., Clawson, M. L., & Laegreid, W. W. (2008). Prevalence of the prion protein gene E211K variant in U.S. cattle. BMC Veterinary Research, 4(25), 1-11.
  • Hizume, M., Kobayashi, A., Teruya, K., Ohashi, H., Ironside, J. W., Mohri, S., & Kitamoto, T. (2008). Human Prion Protein (PrP) 219K Is Converted to PrPScbut Shows Heterozygous Inhibition in Variant Creutzfeldt-Jakob Disease Infection. Journal of Biological Chemistry, 284(6), 3603–3609.
  • Hizume, M., & Mizusawa, H. (2007). [Establishment of the concept of prion diseases]. Nihon Rinsho, 65(8), 1373-1378.
  • Houston, F., & Andréoletti, O. (2019). Animal prion diseases: the risks to human health. Brain Pathology, 29(2), 248–262.
  • Hunter, N. (1998). Scrapie. Molecular Biotechnology, 9(3), 225–234.
  • Hwang, S., & Nicholson, E. M. (2018). Thermodynamic characterization for the denatured state of bovine prion protein and the BSE associated variant E211K. Prion, 12(5-6), 301-309.
  • Iwasaki, Y. (2016). Creutzfeldt-Jakob disease, Neuropathology, 37(2), 174–188.
  • Jacobs, J. G., Bossers, A., Rezaei, H., van Keulen, L. J. M., McCutcheon, S., Sklaviadis, T., Lantier, I., Berthon, P., Lantier, F., van Zijderveld, F. G., & Langeveld, J. P. M. (2011). Proteinase K-resistant material in ARR/VRQ sheep brain affected with classical scrapie is composed mainly of VRQ prion protein. Journal of Virology, 85(23), 12537-12546.
  • Jewell, J. E. (2005). Low frequency of PrP genotype 225SF among free-ranging mule deer (Odocoileus hemionus) with chronic wasting disease. Journal of General Virology, 86(8), 2127–2134.
  • Johnson, C. (2006). Prion protein polymorphisms in white-tailed deer influence susceptibility to chronic wasting disease. Journal of General Virology, 87(7), 2109–2114.
  • Khan, Z., Sankari, A., & Bollu, P.C. (2024) Fatal familial insomnia, StatPearls Publishing, Treasure Island (FL).
  • Kim, Y.-C., & Jeong, B.-H. (2021). The First Meta-Analysis of the M129V Single-Nucleotide Polymorphism (SNP) of the Prion Protein Gene (PRNP) with Sporadic Creutzfeldt-Jakob Disease. Cells, 10(11), 3132.
  • Kim, D. J., Kim, Y. C., Kim, A. D., & Jeong, B. H. (2020). Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (PRNP) in Dogs—A Resistant Animal of Prion Disease. International Journal of Molecular Sciences, 21(11), 4160.
  • Kim, H.H., Kim, Y.C., Kim, K., Kim, A. D., Jeong, B., H. (2021). Novel Polymorphisms and Genetic Features of the Prion Protein Gene (PRNP) in Cats, Hosts of Feline Spongiform Encephalopathy. Genes, 24;12(1):13.
  • Kimberlin, R. H. (1992). Bovine spongiform encephalopathy. Rev Sci Tech, 11(2), 347-489.
  • Kobayashi, A., Teruya, K., Matsuura, Y., Shirai, T., Nakamura, Y., Yamada, M., Mizusawa, H., Mohri, S., & Kitamoto, T. (2015). The influence of PRNP polymorphisms on human prion disease susceptibility: an update. Acta Neuropathologica, 130(2), 159-170.
  • Konold, T., Spiropoulos, J., Chaplin, M. J., Thorne, L., Spencer, Y. I., Wells, G. A. H., & Hawkins, S. A. C. (2009). Transmissibility studies of vacuolar changes in the rostral colliculus of pigs. BMC Veterinary Research, 5(35), 1-13.
  • Kupfer, L., Hinrichs, W., & Groschup, M. H. (2009). Prion protein misfolding. Current Molecular Medicine, 9(7), 826–835.
  • Lacroux, C., Perrin-Chauvineau, C., Corbière, F., Aron, N., Aguilar-Calvo, P., Torres, J. M., Costes, P., Brémaud, I., Lugan, S., Schelcher, F., Barillet, F., & Andréoletti, O. (2014). Genetic resistance to scrapie infection in experimentally challenged goats. Journal of Virology, 88(5), 2406–2413.
  • Lewis, P. A., Tattum, M. H., Jones, S., Bhelt, D., Batchelor, M., Clarke, A. R., Collinge, J., & Jackson, G. S. (2006). Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formation. Journal of General Virology, *87*(Pt 8), 2443–2449.
  • Liberski, P.P. (2012). Historical overview of prion diseases: a view from afar. Folia Neuropathol. 50(1), 1–12.
  • Liberski, P. P., Sikorska, B., & Brown, P. (2012) Kuru: The First Prion Disease. Neurodegenerative Diseases, 143–153.
  • Llorens, F., Rübsamen, N., Hermann, P., Schmitz, M., Villar-Piqué, A., Goebel, S., Karch, A., & Zerr, I. (2020). A prognostic model for overall survival in sporadic Creutzfeldt-Jakob disease. Alzheimer's & Dementia, 16(10), 1438-1447.
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There are 66 citations in total.

Details

Primary Language English
Subjects Veterinary Sciences (Other)
Journal Section Review Articles
Authors

Canan Güven 0009-0005-5882-1295

Iraz Akış Akad 0000-0001-7330-103X

Publication Date April 30, 2025
Submission Date April 7, 2025
Acceptance Date April 25, 2025
Published in Issue Year 2025 Volume: 9 Issue: 1

Cite

APA Güven, C., & Akış Akad, I. (2025). Prion diseases and genetic susceptibility. Journal of Istanbul Veterinary Sciences, 9(1), 65-74.

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