1887

Abstract

Several studies have failed to demonstrate the presence of immune responses to infectious prions during the course of prion disease, reflecting the identical primary structure of normal and disease-associated isoforms and the widespread expression of the normal cellular form of prion protein, PrP, leading to B- and/or T-cell tolerance of disease-associated isoforms and also possibly because antigen-presenting cells are unable to process the highly aggregated, detergent-insoluble, protease-resistant form, PrP. Under certain circumstances, PrP can be revealed to the immune system in immunogenic form, and it has been shown previously that anti-PrP antibodies can be induced to prions immunoadsorbed to Dynabeads using specific anti-PrP monoclonal antibodies, even in PrP-sufficient mice. This study demonstrated in a murine scrapie model that PrP–Dynabeads effectively stimulated the immune system to produce anti-PrP IgM antibodies over prolonged periods after repeated immunization. It was also shown that these immune responses prolonged incubation times in murine scrapie.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/vir.0.005041-0
2009-03-01
2019-11-14
Loading full text...

Full text loading...

/deliver/fulltext/jgv/90/3/777.html?itemId=/content/journal/jgv/10.1099/vir.0.005041-0&mimeType=html&fmt=ahah

References

  1. Beringue, V., Adjou, K. T., Lamoury, F., Maignien, T., Deslys, J. P., Race, R. & Dormont, D. ( 2000; ). Opposite effects of dextran sulfate 500, the polyene antibiotic MS-8209, and Congo red on accumulation of the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent. J Virol 74, 5432–5440.[CrossRef]
    [Google Scholar]
  2. Beringue, V., Vilette, D., Mallinson, G., Archer, F., Kaisar, M., Tayebi, M., Jackson, G. S., Clarke, A. R., Laude, H. & other authors ( 2004; ). PrPSc binding antibodies are potent inhibitors of prion replication in cell lines. J Biol Chem 279, 39671–39676.[CrossRef]
    [Google Scholar]
  3. Bueler, H., Aguzzi, A., Sailer, A., Greiner, R. A., Autenried, P., Aguet, M. & Weissmann, C. ( 1993; ). Mice devoid of PrP are resistant to scrapie. Cell 73, 1339–1347.[CrossRef]
    [Google Scholar]
  4. Dodart, J. C., Bales, K. R. & Paul, S. M. ( 2003; ). Immunotherapy for Alzheimer's disease: will vaccination work? Trends Mol Med 9, 85–87.[CrossRef]
    [Google Scholar]
  5. Eklund, C. M. & Hadlow, W. J. ( 1973; ). Implications of slow viral diseases of domestic animals for human disease. Medicine 52, 357–361.[CrossRef]
    [Google Scholar]
  6. Enari, M., Flechsig, E. & Weissmann, C. ( 2001; ). Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci U S A 98, 9295–9299.[CrossRef]
    [Google Scholar]
  7. Gilch, S., Wopfner, F., Renner-Muller, I., Kremmer, E., Bauer, C., Wolf, E., Brem, G., Groschup, M. H. & Schatzl, H. M. ( 2003; ). Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells. J Biol Chem 278, 18524–18531.[CrossRef]
    [Google Scholar]
  8. Goni, F., Knudsen, E., Schreiber, F., Scholtzova, H., Pankiewicz, J., Carp, R., Meeker, H. C., Rubenstein, R., Brown, D. R. & other authors ( 2005; ). Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience 133, 413–421.[CrossRef]
    [Google Scholar]
  9. Goni, F., Prelli, F., Schreiber, F., Scholtzova, H., Chung, E., Kascsak, R., Brown, D. R., Sigurdsson, E. M., Chabalgoity, J. A. & Wisniewski, T. ( 2008; ). High titers of mucosal and systemic anti-PrP antibodies abrogate oral prion infection in mucosal-vaccinated mice. Neuroscience 153, 679–686.[CrossRef]
    [Google Scholar]
  10. Heppner, F. L., Musahl, C., Arrighi, I., Klein, M. A., Rulicke, T., Oesch, B., Zinkernagel, R. M., Kalinke, U. & Aguzzi, A. ( 2001; ). Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science 294, 178–182.[CrossRef]
    [Google Scholar]
  11. Jones, M., Wight, D., McLoughlin, V., Norrby, K., Ironside, J. W., Connolly, J. G., Farquhar, C. F., Macgregor, I. R. & Head, M. W. ( 2009; ). An antibody to the aggregated synthetic prion protein peptide (PrP106–126) selectively recognizes disease-associated prion protein (PrPSc) from human brain specimens. Brain Pathol (in press). doi:10.1111/j.1750-3639.2008.00181.x
    [Google Scholar]
  12. Kascsak, R. J., Rubenstein, R., Merz, P. A., Tonna DeMasi, M., Fersko, R., Carp, R. I., Wisniewski, H. M. & Diringer, H. ( 1987; ). Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 61, 3688–3693.
    [Google Scholar]
  13. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W. & Glabe, C. G. ( 2003; ). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486–489.[CrossRef]
    [Google Scholar]
  14. Kimberlin, R. H. & Walker, C. A. ( 1979; ). Pathogenesis of scrapie: agent multiplication in brain at the first and second passage of hamster scrapie in mice. J Gen Virol 42, 107–117.[CrossRef]
    [Google Scholar]
  15. Kimberlin, R. H. & Walker, C. A. ( 1988; ). Pathogenesis of experimental scrapie. Ciba Found Symp 135, 37–62.
    [Google Scholar]
  16. Kimberlin, R. H. & Walker, C. A. ( 1989; ). The role of the spleen in the neuroinvasion of scrapie in mice. Virus Res 12, 201–211.[CrossRef]
    [Google Scholar]
  17. McBride, P. A., Eikelenboom, P., Kraal, G., Fraser, H. & Bruce, M. E. ( 1992; ). PrP protein is associated with follicular dendritic cells of spleens and lymph nodes in uninfected and scrapie-infected mice. J Pathol 168, 413–418.[CrossRef]
    [Google Scholar]
  18. Nakamura, N., Miyamoto, K., Shimokawa, M., Nishida, N., Mohri, S., Kitamoto, T., Horiuchi, H., Furusawa, S. & Matsuda, H. ( 2003; ). Generation of antibodies against prion protein by scrapie-infected cell immunization of PrP0/0 mice. Hybrid Hybridomics 22, 263–266.[CrossRef]
    [Google Scholar]
  19. Paramithiotis, E., Pinard, M., Lawton, T., LaBoissiere, S., Leathers, V. L., Zou, W. Q., Estey, L. A., Lamontagne, J., Lehto, M. T. & other authors ( 2003; ). A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 9, 893–899.[CrossRef]
    [Google Scholar]
  20. Peretz, D., Williamson, R. A., Matsunaga, Y., Serban, H., Pinilla, C., Bastidas, R. B., Rozenshteyn, R., James, T. L., Houghten, R. A. & other authors ( 1997; ). A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol 273, 614–622.[CrossRef]
    [Google Scholar]
  21. Peretz, D., Williamson, R. A., Kaneko, K., Vergara, J., Leclerc, E., Schmitt-Ulms, G., Mehlhorn, I. R., Legname, G., Wormald, M. R. & other authors ( 2001; ). Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412, 739–743.[CrossRef]
    [Google Scholar]
  22. Prusiner, S. B., Groth, D., Serban, A., Koehler, R., Foster, D., Torchia, M., Burton, D., Yang, S.-L. & DeArmond, S. J. ( 1993; ). Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci U S A 90, 10608–10612.[CrossRef]
    [Google Scholar]
  23. Rubenstein, R., Kascsak, R. J., Papini, M., Kascsak, R., Carp, R. I., Lafauci, G., Meloen, R. & Langeveld, J. ( 1999; ). Immune surveillance and antigen conformation determines humoral immune response to the prion protein immunogen. J Neurovirol 5, 401–413.[CrossRef]
    [Google Scholar]
  24. Schwarz, A., Kratke, O., Burwinkel, M., Riemer, C., Schultz, J., Henklein, P., Bamme, T. & Baier, M. ( 2003; ). Immunisation with a synthetic prion protein-derived peptide prolongs survival times of mice orally exposed to the scrapie agent. Neurosci Lett 350, 187–189.[CrossRef]
    [Google Scholar]
  25. Sigurdsson, E. M., Brown, D. R., Daniels, M., Kascsak, R. J., Kascsak, R., Carp, R., Meeker, H. C., Frangione, B. & Wisniewski, T. ( 2002; ). Immunization delays the onset of prion disease in mice. Am J Pathol 161, 13–17.[CrossRef]
    [Google Scholar]
  26. Solforosi, L., Criado, J. R., McGavern, D. B., Wirz, S., Sanchez-Alavez, M., Sugama, S., DeGiorgio, L. A., Volpe, B. T., Wiseman, E. & other authors ( 2004; ). Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303, 1514–1516.[CrossRef]
    [Google Scholar]
  27. Spinner, D. S., Kascsak, R. B., Lafauci, G., Meeker, H. C., Ye, X., Flory, M. J., Kim, J. I., Schuller-Levis, G. B., Levis, W. R. & other authors ( 2007; ). CpG oligodeoxynucleotide-enhanced humoral immune response and production of antibodies to prion protein PrPSc in mice immunized with 139A scrapie-associated fibrils. J Leukoc Biol 81, 1374–1385.[CrossRef]
    [Google Scholar]
  28. Tal, Y., Souan, L., Cohen, I. R., Meiner, Z., Taraboulos, A. & Mor, F. ( 2003; ). Complete Freund's adjuvant immunization prolongs survival in experimental prion disease in mice. J Neurosci Res 71, 286–290.[CrossRef]
    [Google Scholar]
  29. Tayebi, M. & Hawke, S. ( 2006; ). Antibody-mediated neuronal apoptosis: therapeutic implications for prion diseases. Immunol Lett 105, 123–126.[CrossRef]
    [Google Scholar]
  30. Tayebi, M., Enever, P., Sattar, Z., Collinge, J. & Hawke, S. ( 2004; ). Disease-associated prion protein elicits immunoglobulin M responses in vivo. Mol Med 10, 104–111.
    [Google Scholar]
  31. Westaway, D. & Carlson, G. A. ( 2002; ). Mammalian prion proteins: enigma, variation and vaccination. Trends Biochem Sci 27, 301–307.[CrossRef]
    [Google Scholar]
  32. White, A. R., Enever, P., Tayebi, M., Mushens, R., Linehan, J., Brandner, S., Anstee, D., Collinge, J. & Hawke, S. ( 2003; ). Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422, 80–83.[CrossRef]
    [Google Scholar]
  33. Williamson, R. A., Peretz, D., Smorodinsky, N., Bastidas, R., Serban, H., Mehlhorn, I., DeArmond, S. J., Prusiner, S. B. & Burton, D. R. ( 1996; ). Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein. Proc Natl Acad Sci U S A 93, 7279–7282.[CrossRef]
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/vir.0.005041-0
Loading
/content/journal/jgv/10.1099/vir.0.005041-0
Loading

Data & Media loading...

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error