Abstract
In a recent monograph on electron microscopy of prion diseases one of us wrote „Attempts, using thin-section transmission electron microscopy, to define the structure of the infectious virus of scrapie (and analogously, Creutzfeldt-Jakob disease, kuru and, recently, bovine spongiform encephalopathy) is an repeatable example of failures, falstarts and misinterpretations.”1 The presence of tubulovesicular structures is, however, a consistent finding.2
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
P.P. Liberski, H. Budka, R. Yanagihara, C.J. Gibbs, and D.C. Gajdusek, Tubulovesicular structures, in: Light and Electron Microscopic Neuropathology of Slow Virus Disorders, P.P. Liberski, CRC Press, Boca Raton, (1992).
M. Jeffrey, I.A. Goodbrand, and M. Goodsir, Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure, Micron. 26: 277 (1995).
P.P. Liberski, and H. Budka, Tubulovesicular structures in Gerstmann-Straussler-Scheinker disease. Acta Neuropathol. (Berl) 88: 491 (1994).
P.P. Liberski, H. Budka, E. Sluga, M. Barcikowska, and H. Kwiecinski, Tubulovesicular structures in Creutzfeldt-Jakob disease. Acta Neuropathol (Berl) 84: 238 (1992).
P.P. Liberski, R. Yanagihara, C.J. Gibbs, Jr, and D.C. Gajdusek, Appearance of tubulovesicular structures in Creutzfeldt-Jakob disease and scrapie precedes the onset of clinical disease. Acta Neuropathol. (Berlin) 79: 349 (1989).
P.P. Liberski, R. Yanagihara, C.J. Gibbs, and D.C. Gajdusek, Tubulovesicular structures in experimental Creutzfeldt-Jakob disease and scrapie. Intervirology 29: 115 (1988).
P.H. Gibson, and L.A. Doughty, An electron microscopic study of inclusion bodies in synaptic terminals of scrapie-infected animals. Acta Neuropathol. (Berl) 77: 420 (1989).
J.F. David-Ferreira, K.L. David-Ferreira, C.J. Gibbs, J.A. and Morris, Scrapie in mice: ultrastructural observations in the cerebral cortex. Proc Soc Exp Biol Med 127: 313 (1968).
J.R. Baringer, and S.B. Prusiner, Experimental scrapie in mice: ultrastructural observations. Ann Neurol 4:205 (1978).
J.R. Baringer, S.B. Prusiner, and J.S. Wong, Scrapie-associated particles in postsynaptic processes. Further ultrastructural studies. J Neuropathol Exp Neurol 40: 281 (1981).
D.C. Gajdusek DC, Infectious amyloids: subacute spongiform encephalopathies as transmissible cerebral amyloidoses, in: „Fields Virology”, 3rd ed, B. Fields, D.M. Knipe, P.M. Howley, eds, Lippincott — Raven Publishers, Philadelphia-New York, (1995).
P.P. Liberski, Prions, β-sheets and transmissible dementias: is ther still something missing? Acta Neuropathol. (Berl) 90: 113 (1995).
S.B. Prusiner, Prions, in: „Fields virology”, 3rd ed, B. Fields, D.M. Knipe, P.M. Howley, eds, Lippincott — Raven Publishers, Philadelphia-New York, (1995).
R.H. Kimberlin, Scrapie and possible relationships with viroids. Sem Virol 1: 153 (1990).
H. Diringer, Hidden amyloidoses. Exp Clin Immunogenet 9:212 (1993).
H.K. Narang, Evidence that scrapie-associated tubulofilamentous particles contain a single stranded DNA. Intervirology 36: 1 (1994).
H.K. Narang, D.M. Asher, and D.C. Gajdusek, Tubulofilaments in negatively stained scrapie-infecetd brains: relationships to scrapie-associated fibrils. Proc. Natl. Acad. Sci. USA. 84: 7730 (1987).
H.K. Narang, D.M. Asher, and D.C. Gajdusek, Evidence that DNA is present in abnormal tubulofilamentous structures found in scrapie. Proc. Natl. Acad. Sci. USA 85: 3375 (1988).
S.J. DeArmond, M.P. McKinley, R.A. Barry, M.B. Braunfeld, J.R. McCulloch, and S.B. Prusiner, Identification of prion filaments in scrapie-infected brain, Cell. 41: 221 (1985).
C.A. Wiley, P.C. Burrola, M.J. Buchmeier, M.K. Wooddell, R.A. Barry, S.B. Prusiner, and P. Lampert, Immuno-gold localization of prion filaments in scrapie-infected hamster brain, Lab Invest. 57: 646 (1987).
P.P. Liberski, D.C. Guiroy, E.S. Williams, R. Yanagihara, P. Brown, and D.C. Gajdusek, The amyloid plaque, in: „Light and Electron Microscopy Neuropathology of Slow Virus Disorders”, P.P. Liberski, ed, CRC Press, Boca Raton, (1993).
P.P. Liberski, and H. Budka, Ultrastructural pathology of Gerstmann-Straussler-Scheinker disease. Ultrastr Pathol 19: 23 (1995).
M. Jeffrey, C. Goodsir, M.E. Bruce, P.A. McBride, and C. Farquhar, Morhogenesis of amyloid plaque in 87V murine scrapie. Neuropathol Appl Neurobiol 20: 535 (1994).
M. Jeffrey, C. Goodsir, M.E. Bruce, P.A. McBride, and W.G. Halliday, Correlative light and electron microscopy studies of PrP localization in 87V scrapie. Brain Res. 656: 329 (1994).
D.A. Kocisko, J.H. Come, S.A. Priola, B. Chesebro, G.J. Raymond, P.T. Lansbury, and B. Caughey, Cell free formation of protease-resistant prion protein. Nature 370: 471 (1994).
R.A. Bessen, D.A. Kocisko, G.J. Raymond, S. Nandan, P.T. Lansbury, and B. Caughey, Non genetic propagation of strain-specific properties of scrapie prion protein, Nature. 375: 698 (1995).
B. Caughey, D.A. Kocisko, G.J. Raymond, P.T. and Lansbury, Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state, Curr Biol.. 2: 807 (1995).
P.T. Lansbury, B. and Caughey, The chemistry of scrapie infection: implications of the „ice 9” metaphor, Curr Biol 2: 1(1995).
M. Barcikowska, P.P. Liberski, J. Boellaard, P. Brown, D.C. Gajdusek, and H. Budka, Microglia is a component of the prion protein amyloid plaque in the Gerstmann-Straussler-Scheinker syndrome. Acta Neuropathol (Berl.) 85: 623 (1993).
D.C. Guiroy, I. Wakayama, P.P. Liberski, and D.C. Gajdusek, Relationship of microglia and scrapie amyloid-immunoreactive plaques in kuru, Creutzfeldt-Jakob disease and Gerstmann-Strausler syndrome. Acta Neuropathol. (Berl) 87: 526 (1994).
D.R. Brown, B. Schmidt, H. Kretzschmar, Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380: 345 (1996).
M.P. McKinley, A. Taraboulos, A. Kenaga, L. Serban, A. Steiber, S.J. DeArmond, and S.B. Prusiner, Ultrastructural localization of scrapie prion proteins of cytoplasmic vesicles of infected cultured cells, Lab. Invest. 65: 622 (1991).
P.A. Merz, R.A. Somerville, H.M. Wisniewski, and J. Iqbal, Abnormal fibrils from scrapie-infected brain. Acta Neuropathol (Berl) 60: 63 (1981).
H. Diringer, H. Gerdelblom, H. Hilmert, M. Ozel M, C. Edelbluth, and R.H. Kimberlin, Scrapie infectivity, fibrils and low molecular weight protein, Nature. 306: 476 (1983).
M.P. McKinley, R.K. Meyer, L. Kenaga, F. Rahbar, R. Cotter, A. Serban, and S.B. Prusiner, Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol 65: 1340 (1991).
Liberski, “Tubulofilamentous particles” are not scrapie-specific and are unrelated to tubulovesicular structures. Acta Neurobiologiae Exp.. 55:149(1995).
D. Chasey, Comment on the paper of H.K. Narang “Evidence that scrapie-associated tubulofilamentous particles contain a single-stranded DNA”. Intervirology. 37:106(1994).
M.P. McKinley, D.C. Bolton, and S.B. Prusiner, A protease resistant protein is a structural component of the scrapie prion, Cell. 35: 57 (1994).
L. Manuelidis, T. Sklaviadis, and E.E. Manuelidis, Evidence suggesting that PrP is not the infectious agent in Creutzfeldt-Jakob disease, EMBO J. 6: 341 (1987).
Y.G. **, L. Ingrosso, and C. Massullo, Amphoterricin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation, Nature. 356: 598 (1992).
R.G. Rohwer, The scrapie agent: “a virus by any other name”, in: Transmissible Spongiform Encephalopathies, Current Topics in Microbiology and Immunology, Vol. 172, B. Chesebro, ed, Springer Verlag, Berlin (1991).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Liberski, P.P., Jeffrey, M., Goodsir, C. (1998). Electron Microscopy in Prion Research: Tubulovesicular Structures Are Not Composed of Prion Protein (PrP) but They May Be Intimately Associated with PrP Amyloid Fibrils. In: Morrison, D.R.O. (eds) Prions and Brain Diseases in Animals and Humans. NATO ASI Series, vol 295. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1896-3_9
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1896-3_9
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1898-7
Online ISBN: 978-1-4899-1896-3
eBook Packages: Springer Book Archive