Susceptibility of Common Fibroblast Cell Lines to Transmissible Spongiform Encephalopathy Agents

Journal of Infectious Diseases

Volumn 189, Issue 3, 2004, Pages 431-439

  Vorberg, Ina ^a   Raines, Anne ^a   Story, Brian ^b   Priola, Suzette A ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

ANIMAL CELL; ANIMAL PRODUCT; ARTICLE; BRAIN INFECTION; CELLULAR DISTRIBUTION; CONTAMINATION; CONTROLLED STUDY; DISEASE PREDISPOSITION; FIBROBLAST CULTURE; MOUSE; NONHUMAN; PREDICTION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION; SCRAPIE;

3T3 CELLS; ANIMALS; CLONE CELLS; FIBROBLASTS; MICE; MICE, INBRED C57BL; PRIONS; PRPC PROTEINS; PRPSC PROTEINS;

EID: 1142285202     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/381166     Document Type: Article

References (43)

1. Pan KM, Baldwin M, Nguyen J, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90:10962-6.
2. Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-321). Nature 1996; 382:180-2.
3. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44.
4. Caughey B, Chesebro B. Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol 1997; 7:56-62.
5. Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363-83.
6. Oesch B, Westaway D, Walchli M, et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985; 40:735-46.
7. Harris DA, Lele P, Snider WD. Localization of the mRNA for a chicken prion protein by in situ hybridization. Proc Natl Acad Sci USA 1993; 90:4309-13.
8. Pammer J, Suchy A, Rendl M, Tschachler E. Cellular prion protein expressed by bovine squamous epithelia of skin and upper gastrointestinal tract. Lancet 1999; 354:1702-3.
9. Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 1982; 218:1309-11.
10. Kitamoto T, Muramoto T, Mohri S, Doh-Ura K, Tateishi J. Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jakob disease. J Virol 1991; 65:6292-5.
11. Clarke MC, Millson GC. Infection of a cell line of mouse L fibroblasts with scrapie agent. Nature 1976; 261:144-5.
12. Rubenstein R, Carp RI, Callahan SM. In vitro replication of scrapie agent in a neuronal model: infection of PC12 cells. J Gen Virol 1984; 65:2191-8.
13. Race RE, Fadness LH, Chesebro B. Characterization of scrapie infection in mouse neuroblastoma cells. J Gen Virol 1987; 68:1391-9.
14. Butler DA, Scott MR, Bockman JM, et al. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J Virol 1988; 62:1558-64.
15. Taraboulos A, Serban D, Prusiner SB. Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J Cell Biol 1990; 110:2117-32.
16. Schatzl HM, Laszlo L, Holtzman DM, et al. A hypothalamic neuronal cell line persistently infected with scrapie prions exhibits apoptosis. J Virol 1997; 71:8821-31.
17. Vilette D, Andreoletti O, Archer F, et al. Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein. Proc Natl Acad Sci USA 2001; 98:4055-9.
18. Follet J, Lemaire-Vieille C, Blanquet-Grossard F, et al. PrP expression and replication by Schwann cells: implications in prion spreading. J Virol 2002; 76:2434-9.
19. Gibson PE, Bell TM, Field EJ. Failure of the scrapie agent to replicate in L5178Y mouse leukaemic cells. Res Vet Sci 1972; 13:95-6.
20. Hunter N, Foster J, Chong A, et al. Transmission of prion diseases by blood transfusion. J Gen Virol 2002; 83:2897-905.
21. Houston F, Foster JD, Chong A, Hunter N, Bostock CJ. Transmission of BSE by blood transfusion in sheep. Lancet 2000; 356:999-1000.
22. Clarke MC, Haig DA. Evidence for the multiplication of scrapie agent in cell culture. Nature 1970; 225:100-1.
23. Cashman NR. Transmissible spongiform encephalopathies: vaccine issues. Dev Biol (Basel) 2001; 106:455-9.
24. Cherednichenko Y, Fadeeva LL, Sologub VK. Antigenic changes in the cells latently infected with the scrapie agent. Acta Virol 1985; 29:515.
25. Nishida N, Harris DA, Vilette D, et al. Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J Virol 2000; 74:320-5.
26. Kascsak RJ, Rubenstein R, Merz PA, et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 1987; 61:3688-93.
27. Vorberg I, Groschup MH, Pfaff E, Priola SA. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J Virol 2003; 77:2003-9.
28. Mann R, Mulligan RC, Baltimore D. Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus. Cell 1983; 33:153-9.
29. Miller AD, Buttimore C. Redesign of retrovirus packaging cell lines to avoid recombination leading to helper virus production. Mol Cell Biol 1986; 6:2895-902.
30. Priola SA, Caughey B, Race RE, Chesebro B. Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. J Virol 1994; 68:4873-8.
31. Bruce ME. Scrapie strain variation and mutation. Br Med Bull 1993; 49:822-38.
32. Vorberg I, Priola SA. Molecular basis of scrapie strain glycoform variation. J Biol Chem 2002; 277:36775-81.
33. Vorberg I, Chan K, Priola SA. Deletion of β-strand and α-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform. J Virol 2001; 75:10024-32.
34. Gilch S, Winklhofer KF, Groschup MH, et al. Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease. EMBO J 2001; 20:3957-66.
35. Bradley R. Bovine spongiform encephalopathy distribution and update on some transmission and decontamination studies. In: Bovine spongiform encephalopathy - the BSE dilemma: Serone Symposia USA. Norwell, MA: Serone Symposia USA and the National Institute of Neurological Disorders and Stroke, National Institutes of Health, 1996:11-27.
36. Meiner Z, Halimi M, Polakiewicz RD, Prusiner SB, Gabizon R. Presence of prion protein in peripheral tissues of Libyan Jews with Creutzfeldt-Jakob disease. Neurology 1992; 42:1355-60.
37. Race RE, Caughey B, Graham K, Ernst D, Chesebro B. Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cell clones. J Virol 1988; 62:2845-9.
38. Bosque PJ, Prusiner SB. Cultured cell sublines highly susceptible to prion infection. J Virol 2000; 74:4377-86.
39. Rheinwald JG, Green H. Serial cultivation of strains of human epidermal keratinocytes: the formation of keratinizing colonies from single cells. Cell 1975; 6:331-44.
40. Matouskova E, McKay I, Povysil C, Konigova R, Chaloupkova A, Vesely P. Characterization of the differentiated phenotype of an organotypic model of skin derived from human keratinocytes and dried porcine dermis. Folia Biol (Praha) 1998; 44:59-66.
41. The Centers for Disease Control and Prevention. Public Health Service recommendations for the use of vaccines manufactured with bovine-derived materials. JAMA 2001; 285:532.
42. The European Agency for the Evaluation of Medicinal Products. Questions and answers on bovine spongiform encephalopathies (BSE) and vaccines. Available at http://www.emea.eu.int/pdfs/human/bwp/081901en.pdf. Accessed 13 January 2003.
43. Bruce M, Chree A, McConnell I, Foster J, Pearson G, Fraser H. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B Biol Sci 1994; 343:405-11.