Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion
Abstract
:1. Introduction
2. PrP Conversion
2.1. PrPC and PrPSc
2.2. In Vitro PrP Conversion
2.3. Seeded-Polymerization Mechanism in PrP Conversion
3. Virus Infections in PrP Conversion
3.1. Neurotropic IAV Infection in PrP Conversion
3.2. Other Virus Infections in Prion Infection
4. Tg Mouse Models of Hereditary Prion Diseases
4.1. Genetic Mutations in PrP Conversion
4.2. Tg Mouse Models of GSS
4.3. Tg Mouse Models of fCJD
4.4. Tg Mouse Models of FFI
5. Reverse Genetic Studies for Acquired Prion Diseases
5.1. The N-Terminal Polybasic Residues of PrPC in Prion Infection
5.2. The Central Residues of PrPC in Prion Infection
6. Perspectives
Author Contributions
Funding
Conflicts of Interest
References
- Prusiner, S.B. Prions. Proc. Natl. Acad. Sci. USA 1998, 95, 13363–13383. [Google Scholar] [CrossRef] [Green Version]
- DeArmond, S.J.; Prusiner, S.B. Etiology and pathogenesis of prion diseases. Am. J. Pathol. 1995, 146, 785–811. [Google Scholar] [PubMed]
- Scheckel, C.; Aguzzi, A. Prions, prionoids and protein misfolding disorders. Nat. Rev. Genet. 2018, 19, 405–418. [Google Scholar] [CrossRef] [Green Version]
- Brandel, J.P.; Peckeu, L.; Haik, S. The French surveillance network of Creutzfeldt-Jakob disease. Epidemiological data in France and worldwide. Transfus. Clin. Biol. 2013, 20, 395–397. [Google Scholar] [CrossRef] [PubMed]
- Heinemann, U.; Krasnianski, A.; Meissner, B.; Varges, D.; Kallenberg, K.; Schulz-Schaeffer, W.J.; Steinhoff, B.J.; Grasbon-Frodl, E.M.; Kretzschmar, H.A.; Zerr, I. Creutzfeldt-Jakob disease in Germany: A prospective 12-year surveillance. Brain 2007, 130, 1350–1359. [Google Scholar] [CrossRef] [Green Version]
- Maddox, R.A.; Person, M.K.; Blevins, J.E.; Abrams, J.Y.; Appleby, B.S.; Schonberger, L.B.; Belay, E.D. Prion disease incidence in the United States: 2003–2015. Neurology 2020, 94, e153–e157. [Google Scholar] [CrossRef] [PubMed]
- Uttley, L.; Carroll, C.; Wong, R.; Hilton, D.A.; Stevenson, M. Creutzfeldt-Jakob disease: A systematic review of global incidence, prevalence, infectivity, and incubation. Lancet Infect. Dis. 2020, 20, e2–e10. [Google Scholar] [CrossRef]
- Webb, T.E.; Poulter, M.; Beck, J.; Uphill, J.; Adamson, G.; Campbell, T.; Linehan, J.; Powell, C.; Brandner, S.; Pal, S.; et al. Phenotypic heterogeneity and genetic modification of P102L inherited prion disease in an international series. Brain 2008, 131, 2632–2646. [Google Scholar] [CrossRef] [Green Version]
- Cracco, L.; Appleby, B.S.; Gambetti, P. Fatal familial insomnia and sporadic fatal insomnia. Handb. Clin. Neurol. 2018, 153, 271–299. [Google Scholar]
- Will, R.G.; Ironside, J.W.; Zeidler, M.; Cousens, S.N.; Estibeiro, K.; Alperovitch, A.; Poser, S.; Pocchiari, M.; Hofman, A.; Smith, P.G. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 1996, 347, 921–925. [Google Scholar] [CrossRef]
- Will, R.G. Acquired prion disease: Iatrogenic CJD, variant CJD, kuru. Br. Med. Bull. 2003, 66, 255–265. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wells, G.A.; Scott, A.C.; Johnson, C.T.; Gunning, R.F.; Hancock, R.D.; Jeffrey, M.; Dawson, M.; Bradley, R. A novel progressive spongiform encephalopathy in cattle. Vet. Rec. 1987, 121, 419–420. [Google Scholar] [CrossRef] [PubMed]
- Orge, L.; Lima, C.; Machado, C.; Tavares, P.; Mendonca, P.; Carvalho, P.; Silva, J.; Pinto, M.L.; Bastos, E.; Pereira, J.C.; et al. Neuropathology of Animal Prion Diseases. Biomolecules 2021, 11, 466. [Google Scholar] [CrossRef] [PubMed]
- Williams, E.S.; Young, S. Spongiform encephalopathy of Rocky Mountain elk. J. Wildl. Dis. 1982, 18, 465–471. [Google Scholar] [CrossRef]
- Wilson, R.; Plinston, C.; Hunter, N.; Casalone, C.; Corona, C.; Tagliavini, F.; Suardi, S.; Ruggerone, M.; Moda, F.; Graziano, S.; et al. Chronic wasting disease and atypical forms of bovine spongiform encephalopathy and scrapie are not transmissible to mice expressing wild-type levels of human prion protein. J. Gen. Virol. 2012, 93, 1624–1629. [Google Scholar] [CrossRef]
- Belay, E.D.; Maddox, R.A.; Williams, E.S.; Miller, M.W.; Gambetti, P.; Schonberger, L.B. Chronic wasting disease and potential transmission to humans. Emerg. Infect. Dis. 2004, 10, 977–984. [Google Scholar] [CrossRef] [Green Version]
- Belay, E.D.; Gambetti, P.; Schonberger, L.B.; Parchi, P.; Lyon, D.R.; Capellari, S.; McQuiston, J.H.; Bradley, K.; Dowdle, G.; Crutcher, J.M.; et al. Creutzfeldt-Jakob disease in unusually young patients who consumed venison. Arch. Neurol. 2001, 58, 1673–1678. [Google Scholar] [CrossRef]
- Brown, P.; Cathala, F.; Raubertas, R.F.; Gajdusek, D.C.; Castaigne, P. The epidemiology of Creutzfeldt-Jakob disease: Conclusion of a 15-year investigation in France and review of the world literature. Neurology 1987, 37, 895–904. [Google Scholar] [CrossRef]
- Van Duijn, C.M.; Delasnerie-Laupretre, N.; Masullo, C.; Zerr, I.; de Silva, R.; Wientjens, D.P.; Brandel, J.P.; Weber, T.; Bonavita, V.; Zeidler, M.; et al. Case-control study of risk factors of Creutzfeldt-Jakob disease in Europe during 1993-95. European Union (EU) Collaborative Study Group of Creutzfeldt-Jakob disease (CJD). Lancet 1998, 351, 1081–1085. [Google Scholar] [CrossRef]
- Bueler, H.; Aguzzi, A.; Sailer, A.; Greiner, R.A.; Autenried, P.; Aguet, M.; Weissmann, C. Mice devoid of PrP are resistant to scrapie. Cell 1993, 73, 1339–1347. [Google Scholar] [CrossRef]
- Prusiner, S.B.; Groth, D.; Serban, A.; Koehler, R.; Foster, D.; Torchia, M.; Burton, D.; Yang, S.L.; DeArmond, S.J. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA 1993, 90, 10608–10612. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Manson, J.C.; Clarke, A.R.; McBride, P.A.; McConnell, I.; Hope, J. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 1994, 3, 331–340. [Google Scholar]
- Sakaguchi, S.; Katamine, S.; Shigematsu, K.; Nakatani, A.; Moriuchi, R.; Nishida, N.; Kurokawa, K.; Nakaoke, R.; Sato, H.; Jishage, K.; et al. Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent. J. Virol. 1995, 69, 7586–7592. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hara, H.; Chida, J.; Uchiyama, K.; Pasiana, A.D.; Takahashi, E.; Kido, H.; Sakaguchi, S. Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells. Sci. Rep. 2021, 11, 10109. [Google Scholar] [CrossRef]
- Oesch, B.; Westaway, D.; Walchli, M.; McKinley, M.P.; Kent, S.B.; Aebersold, R.; Barry, R.A.; Tempst, P.; Teplow, D.B.; Hood, L.E.; et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985, 40, 735–746. [Google Scholar] [CrossRef]
- Prusiner, S.B. Molecular biology of prion diseases. Science 1991, 252, 1515–1522. [Google Scholar] [CrossRef] [Green Version]
- Hackl, S.; Becker, C.F.W. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications. J. Pept. Sci. 2019, 25, e3216. [Google Scholar] [CrossRef]
- Aguzzi, A.; Baumann, F.; Bremer, J. The prion’s elusive reason for being. Annu. Rev. Neurosci. 2008, 31, 439–477. [Google Scholar] [CrossRef]
- Chida, J.; Hara, H.; Yano, M.; Uchiyama, K.; Das, N.R.; Takahashi, E.; Miyata, H.; Tomioka, Y.; Ito, T.; Kido, H.; et al. Prion protein protects mice from lethal infection with influenza A viruses. PLoS Pathog. 2018, 14, e1007049. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chida, J.; Hara, H.; Uchiyama, K.; Takahashi, E.; Miyata, H.; Kosako, H.; Tomioka, Y.; Ito, T.; Horiuchi, H.; Matsuda, H.; et al. Prion protein signaling induces M2 macrophage polarization and protects from lethal influenza infection in mice. PLoS Pathog. 2020, 16, e1008823. [Google Scholar] [CrossRef]
- Prusiner, S.B. The prion diseases. Brain Pathol. 1998, 8, 499–513. [Google Scholar] [CrossRef] [PubMed]
- Prusiner, S.B.; McKinley, M.P.; Bowman, K.A.; Bolton, D.C.; Bendheim, P.E.; Groth, D.F.; Glenner, G.G. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983, 35, 349–358. [Google Scholar] [CrossRef]
- Pan, K.M.; Baldwin, M.; Nguyen, J.; Gasset, M.; Serban, A.; Groth, D.; Mehlhorn, I.; Huang, Z.; Fletterick, R.J.; Cohen, F.E.; et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 1993, 90, 10962–10966. [Google Scholar] [CrossRef] [Green Version]
- Kocisko, D.A.; Come, J.H.; Priola, S.A.; Chesebro, B.; Raymond, G.J.; Lansbury, P.T.; Caughey, B. Cell-free formation of protease-resistant prion protein. Nature 1994, 370, 471–474. [Google Scholar] [CrossRef]
- Saborio, G.P.; Permanne, B.; Soto, C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001, 411, 810–813. [Google Scholar] [CrossRef]
- Castilla, J.; Saa, P.; Hetz, C.; Soto, C. In vitro generation of infectious scrapie prions. Cell 2005, 121, 195–206. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Legname, G.; Baskakov, I.V.; Nguyen, H.O.; Riesner, D.; Cohen, F.E.; DeArmond, S.J.; Prusiner, S.B. Synthetic mammalian prions. Science 2004, 305, 673–676. [Google Scholar] [CrossRef]
- Wang, F.; Wang, X.; Yuan, C.G.; Ma, J. Generating a prion with bacterially expressed recombinant prion protein. Science 2010, 327, 1132–1135. [Google Scholar] [CrossRef] [Green Version]
- Fernandez-Borges, N.; Di Bari, M.A.; Erana, H.; Sanchez-Martin, M.; Pirisinu, L.; Parra, B.; Elezgarai, S.R.; Vanni, I.; Lopez-Moreno, R.; Vaccari, G.; et al. Cofactors influence the biological properties of infectious recombinant prions. Acta Neuropathol. 2018, 135, 179–199. [Google Scholar] [CrossRef]
- Prusiner, S.B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216, 136–144. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bolton, D.C.; McKinley, M.P.; Prusiner, S.B. Identification of a protein that purifies with the scrapie prion. Science 1982, 218, 1309–1311. [Google Scholar] [CrossRef]
- Jarrett, J.T.; Lansbury, P.T., Jr. Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer’s disease and scrapie? Cell 1993, 73, 1055–1058. [Google Scholar] [CrossRef]
- Silveira, J.R.; Raymond, G.J.; Hughson, A.G.; Race, R.E.; Sim, V.L.; Hayes, S.F.; Caughey, B. The most infectious prion protein particles. Nature 2005, 437, 257–261. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wille, H.; Bian, W.; McDonald, M.; Kendall, A.; Colby, D.W.; Bloch, L.; Ollesch, J.; Borovinskiy, A.L.; Cohen, F.E.; Prusiner, S.B.; et al. Natural and synthetic prion structure from X-ray fiber diffraction. Proc. Natl. Acad. Sci. USA 2009, 106, 16990–16995. [Google Scholar] [CrossRef] [Green Version]
- Vazquez-Fernandez, E.; Vos, M.R.; Afanasyev, P.; Cebey, L.; Sevillano, A.M.; Vidal, E.; Rosa, I.; Renault, L.; Ramos, A.; Peters, P.J.; et al. The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy. PLoS Pathog. 2016, 12, e1005835. [Google Scholar] [CrossRef] [PubMed]
- Spagnolli, G.; Rigoli, M.; Orioli, S.; Sevillano, A.M.; Faccioli, P.; Wille, H.; Biasini, E.; Requena, J.R. Full atomistic model of prion structure and conversion. PLoS Pathog. 2019, 15, e1007864. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Baskakov, I.V.; Caughey, B.; Requena, J.R.; Sevillano, A.M.; Surewicz, W.K.; Wille, H. The prion 2018 round tables (I): The structure of PrPSc. Prion 2019, 13, 46–52. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Groveman, B.R.; Dolan, M.A.; Taubner, L.M.; Kraus, A.; Wickner, R.B.; Caughey, B. Parallel in-register intermolecular beta-sheet architectures for prion-seeded prion protein (PrP) amyloids. J. Biol. Chem. 2014, 289, 24129–24142. [Google Scholar] [CrossRef] [Green Version]
- Ferhadian, D.; Contrant, M.; Printz-Schweigert, A.; Smyth, R.P.; Paillart, J.C.; Marquet, R. Structural and Functional Motifs in Influenza Virus RNAs. Front. Microbiol. 2018, 9, 559. [Google Scholar] [CrossRef] [Green Version]
- Adler, V.; Zeiler, B.; Kryukov, V.; Kascsak, R.; Rubenstein, R.; Grossman, A. Small, highly structured RNAs participate in the conversion of human recombinant PrPSen to PrPRes in vitro. J. Mol. Biol. 2003, 332, 47–57. [Google Scholar] [CrossRef]
- Deleault, N.R.; Lucassen, R.W.; Supattapone, S. RNA molecules stimulate prion protein conversion. Nature 2003, 425, 717–720. [Google Scholar] [CrossRef] [PubMed]
- Ehresmann, D.W.; Hogan, R.N. Acceleration of scrapie disease in mice by an adenovirus. Intervirology 1986, 25, 103–110. [Google Scholar] [CrossRef]
- Stanton, J.B.; Knowles, D.P.; O’Rourke, K.I.; Herrmann-Hoesing, L.M.; Mathison, B.A.; Baszler, T.V. Small-ruminant lentivirus enhances PrPSc accumulation in cultured sheep microglial cells. J. Virol. 2008, 82, 9839–9847. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Haviv, Y.; Avrahami, D.; Ovadia, H.; Ben-Hur, T.; Gabizon, R.; Sharon, R. Induced neuroprotection independently from PrPSc accumulation in a mouse model for prion disease treated with simvastatin. Arch. Neurol. 2008, 65, 762–775. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Leblanc, P.; Alais, S.; Porto-Carreiro, I.; Lehmann, S.; Grassi, J.; Raposo, G.; Darlix, J.L. Retrovirus infection strongly enhances scrapie infectivity release in cell culture. EMBO J. 2006, 25, 2674–2685. [Google Scholar] [CrossRef] [Green Version]
- Watts, J.C.; Prusiner, S.B. Experimental Models of Inherited PrP Prion Diseases. Cold Spring Harb. Perspect. Med. 2017, 7, a02715. [Google Scholar] [CrossRef] [PubMed]
- Hsiao, K.K.; Scott, M.; Foster, D.; Groth, D.F.; DeArmond, S.J.; Prusiner, S.B. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 1990, 250, 1587–1590. [Google Scholar] [CrossRef] [PubMed]
- Hsiao, K.K.; Groth, D.; Scott, M.; Yang, S.L.; Serban, H.; Rapp, D.; Foster, D.; Torchia, M.; Dearmond, S.J.; Prusiner, S.B. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. USA 1994, 91, 9126–9130. [Google Scholar] [CrossRef] [Green Version]
- Yang, W.; Cook, J.; Rassbach, B.; Lemus, A.; DeArmond, S.J.; Mastrianni, J.A. A New Transgenic Mouse Model of Gerstmann-Straussler-Scheinker Syndrome Caused by the A117V Mutation of PRNP. J. Neurosci. 2009, 29, 10072–10080. [Google Scholar] [CrossRef] [Green Version]
- Chiesa, R.; Piccardo, P.; Ghetti, B.; Harris, D.A. Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 1998, 21, 1339–1351. [Google Scholar] [CrossRef] [Green Version]
- Chiesa, R.; Drisaldi, B.; Quaglio, E.; Migheli, A.; Piccardo, P.; Ghetti, B.; Harris, D.A. Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proc. Natl. Acad. Sci. USA 2000, 97, 5574–5579. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Biasini, E.; Seegulam, M.E.; Patti, B.N.; Solforosi, L.; Medrano, A.Z.; Christensen, H.M.; Senatore, A.; Chiesa, R.; Williamson, R.A.; Harris, D.A. Non-infectious aggregates of the prion protein react with several PrPSc-directed antibodies. J. Neurochem. 2008, 105, 2190–2204. [Google Scholar] [CrossRef]
- Friedman-Levi, Y.; Meiner, Z.; Canello, T.; Frid, K.; Kovacs, G.G.; Budka, H.; Avrahami, D.; Gabizon, R. Fatal prion disease in a mouse model of genetic E200K Creutzfeldt-Jakob disease. PLoS Pathog. 2011, 7, e1002350. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Asante, E.A.; Gowland, I.; Grimshaw, A.; Linehan, J.M.; Smidak, M.; Houghton, R.; Osiguwa, O.; Tomlinson, A.; Joiner, S.; Brandner, S.; et al. Absence of spontaneous disease and comparative prion susceptibility of transgenic mice expressing mutant human prion proteins. J. Gen. Virol. 2009, 90, 546–558. [Google Scholar] [CrossRef]
- Jackson, W.S.; Borkowski, A.W.; Watson, N.E.; King, O.D.; Faas, H.; Jasanoff, A.; Lindquist, S. Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases. Proc. Natl. Acad. Sci. USA 2013, 110, 14759–14764. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Dossena, S.; Imeri, L.; Mangieri, M.; Garofoli, A.; Ferrari, L.; Senatore, A.; Restelli, E.; Balducci, C.; Fiordaliso, F.; Salio, M.; et al. Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model. Neuron 2008, 60, 598–609. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Bouybayoune, I.; Mantovani, S.; Del Gallo, F.; Bertani, I.; Restelli, E.; Comerio, L.; Tapella, L.; Baracchi, F.; Fernandez-Borges, N.; Mangieri, M.; et al. Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease. PLoS Pathog. 2015, 11, e1004796. [Google Scholar] [CrossRef]
- Jackson, W.S.; Borkowski, A.W.; Faas, H.; Steele, A.D.; King, O.D.; Watson, N.; Jasanoff, A.; Lindquist, S. Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. Neuron 2009, 63, 438–450. [Google Scholar] [CrossRef] [Green Version]
- Fischer, M.; Rulicke, T.; Raeber, A.; Sailer, A.; Moser, M.; Oesch, B.; Brandner, S.; Aguzzi, A.; Weissmann, C. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 1996, 15, 1255–1264. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Turnbaugh, J.A.; Unterberger, U.; Saa, P.; Massignan, T.; Fluharty, B.R.; Bowman, F.P.; Miller, M.B.; Supattapone, S.; Biasini, E.; Harris, D.A. The N-terminal, polybasic region of PrPC dictates the efficiency of prion propagation by binding to PrPSc. J. Neurosci. 2012, 32, 8817–8830. [Google Scholar] [CrossRef] [Green Version]
- Das, N.R.; Miyata, H.; Hara, H.; Chida, J.; Uchiyama, K.; Masujin, K.; Watanabe, H.; Kondoh, G.; Sakaguchi, S. The N-Terminal Polybasic Region of Prion Protein Is Crucial in Prion Pathogenesis Independently of the Octapeptide Repeat Region. Mol. Neurobiol. 2020, 57, 1203–1216. [Google Scholar] [CrossRef] [PubMed]
- Flechsig, E.; Shmerling, D.; Hegyi, I.; Raeber, A.J.; Fischer, M.; Cozzio, A.; von Mering, C.; Aguzzi, A.; Weissmann, C. Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 2000, 27, 399–408. [Google Scholar] [CrossRef] [Green Version]
- Weissmann, C.; Flechsig, E. PrP knock-out and PrP transgenic mice in prion research. Br. Med. Bull. 2003, 66, 43–60. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hara, H.; Miyata, H.; Das, N.R.; Chida, J.; Yoshimochi, T.; Uchiyama, K.; Watanabe, H.; Kondoh, G.; Yokoyama, T.; Sakaguchi, S. Prion Protein Devoid of the Octapeptide Repeat Region Delays Bovine Spongiform Encephalopathy Pathogenesis in Mice. J. Virol. 2018, 92, e01368-17. [Google Scholar] [CrossRef] [Green Version]
- Uchiyama, K.; Miyata, H.; Yamaguchi, Y.; Imamura, M.; Okazaki, M.; Pasiana, A.D.; Chida, J.; Hara, H.; Atarashi, R.; Watanabe, H.; et al. Strain-Dependent Prion Infection in Mice Expressing Prion Protein with Deletion of Central Residues 91–106. Int. J. Mol. Sci. 2020, 21, 7260. [Google Scholar] [CrossRef] [PubMed]
- Hara, H.; Okemoto-Nakamura, Y.; Shinkai-Ouchi, F.; Hanada, K.; Yamakawa, Y.; Hagiwara, K. Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrPC to PrPSc in prion-infected neuroblastoma cells. J. Virol. 2012, 86, 5626–5636. [Google Scholar] [CrossRef] [Green Version]
- Hagiwara, K.; Hara, H.; Hanada, K. Species-barrier phenomenon in prion transmissibility from a viewpoint of protein science. J. Biochem. 2013, 153, 139–145. [Google Scholar] [CrossRef] [PubMed]
- Govaerts, C.; Wille, H.; Prusiner, S.B.; Cohen, F.E. Evidence for assembly of prions with left-handed beta-helices into trimers. Proc. Natl. Acad. Sci. USA 2004, 101, 8342–8347. [Google Scholar] [CrossRef] [Green Version]
- Kraus, A.; Hoyt, F.; Schwartz, C.L.; Hansen, B.; Artikis, E.; Hughson, A.G.; Raymond, G.J.; Race, B.; Baron, G.S.; Caughey, B. High-resolution structure and strain comparison of infectious mammalian prions. Mol. Cell 2021, 81, 4540–4551. [Google Scholar] [CrossRef]
Hereditary Prion Diseases | Mutant PrPs | Conversion to Neurotoxic PrPSc/Infectious PrPSc | References |
---|---|---|---|
GSS | Mo-PrP-P101L | Yes/Yes | [57,58] |
Mo-PrP-A116V | Yes/N.D. | [59] | |
Mo-PrP-PG14 | Yes/No | [60,61,62] | |
fCJD | Mo/Hu-PrP-E199K | Yes/Yes | [63] |
Hu-PrP-E200K | No/No | [64] | |
Mo-PrP-E199K(3F4) | Yes/Yes | [65] | |
Mo-PrP-D177N(V128) | Yes/No | [66] | |
FFI | Mo-PrP-D177N(M128) | Yes/No | [67] |
Mo-PrP-D177N(M128)(3F4) | Yes/Yes | [68] |
PrPs | Susceptibility to Prions | References |
---|---|---|
PrP∆23–31 | Reduced to RML prions | [70] |
PrP3K3A | Reduced to RML and 22L prions | [71] |
PrP∆32–80 | Not reduced to RML prions | [72] |
PrP∆32–93 | Reduced to RML prions | [73] |
PrP∆32–106 | Resistant to RML prions | [73] |
PrP∆OR | Not reduced to RML and 22L prions Reduced to BSE prions | [74] |
PrP∆91–106 | Resistant to RML and 22L prions Reduced to BSE prions | [75] |
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. |
© 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Hara, H.; Sakaguchi, S. Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion. Int. J. Mol. Sci. 2021, 22, 12439. https://doi.org/10.3390/ijms222212439
Hara H, Sakaguchi S. Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion. International Journal of Molecular Sciences. 2021; 22(22):12439. https://doi.org/10.3390/ijms222212439
Chicago/Turabian StyleHara, Hideyuki, and Suehiro Sakaguchi. 2021. "Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion" International Journal of Molecular Sciences 22, no. 22: 12439. https://doi.org/10.3390/ijms222212439