This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Supattapone, S.
Right arrow Articles by Scott, M. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Supattapone, S.
Right arrow Articles by Scott, M. R.

 Previous Article  |  Next Article 

Journal of Virology, February 2001, p. 1408-1413, Vol. 75, No. 3
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.3.1408-1413.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of Two Prion Protein Regions That Modify Scrapie Incubation Time

Surachai Supattapone,1,2 Tamaki Muramoto,2,dagger Giuseppe Legname,1,2 Ingrid Mehlhorn,2,Dagger Fred E. Cohen,1,3,4,5 Stephen J. DeArmond,1,6 Stanley B. Prusiner,1,2,5 and Michael R. Scott1,2,*

Institute for Neurodegenerative Diseases1 and Departments of Neurology,2 Medicine,3 Pharmaceutical Chemistry,4 Biochemistry and Biophysics,5 and Pathology,6 University of California, San Francisco, California 94143

Received 8 August 2000/Accepted 23 October 2000

A series of prion transmission experiments was performed in transgenic (Tg) mice expressing either wild-type, chimeric, or truncated prion protein (PrP) molecules. Following inoculation with Rocky Mountain Laboratory (RML) murine prions, scrapie incubation times for Tg(MoPrP)4053, Tg(MHM2)294/Prnp0/0, and Tg(MoPrP,Delta 23-88)9949/Prnp0/0 mice were ~50, 120, and 160 days, respectively. Similar scrapie incubation times were obtained after inoculation of these lines of Tg mice with either MHM2(MHM2(RML)) or MoPrP(Delta 23-88)(RML) prions, excluding the possibility that sequence-dependent transmission barriers could account for the observed differences. Tg(MHM2)294/Prnp0/0 mice displayed prolonged scrapie incubation times with four different strains of murine prions. These data provide evidence that the N terminus of MoPrP and the chimeric region of MHM2 PrP (residues 108 through 111) both influence the inherent efficiency of prion propagation.

* Corresponding author. Mailing address: Institute for Neurodegenerative Diseases, Box 0518, University of California, San Francisco, CA 94143-0518. Phone: (415) 476-4482. Fax: (415) 476-8386.

dagger Present address: Department of Neurological Science, Tohoku University School of Medicine, Aoba-ku, Sendai, Japan 980-8575.

Dagger Present address: Montclair Group, Tal Biosciences, Alameda, CA 94501.

Journal of Virology, February 2001, p. 1408-1413, Vol. 75, No. 3
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.3.1408-1413.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Chiesa, R., Piccardo, P., Biasini, E., Ghetti, B., Harris, D. A. (2008). Aggregated, Wild-Type Prion Protein Causes Neurological Dysfunction and Synaptic Abnormalities. J. Neurosci. 28: 13258-13267 [Abstract] [Full Text]  
  • Deleault, A. M., Deleault, N. R., Harris, B. T., Rees, J. R., Supattapone, S. (2008). The effects of prion protein proteolysis and disaggregation on the strain properties of hamster scrapie. J. Gen. Virol. 89: 2642-2650 [Abstract] [Full Text]  
  • Colby, D. W., Zhang, Q., Wang, S., Groth, D., Legname, G., Riesner, D., Prusiner, S. B. (2007). Prion detection by an amyloid seeding assay. Proc. Natl. Acad. Sci. USA 104: 20914-20919 [Abstract] [Full Text]  
  • Lau, A. L., Yam, A. Y., Michelitsch, M. M. D., Wang, X., Gao, C., Goodson, R. J., Shimizu, R., Timoteo, G., Hall, J., Medina-Selby, A., Coit, D., McCoin, C., Phelps, B., Wu, P., Hu, C., Chien, D., Peretz, D. (2007). Characterization of prion protein (PrP)-derived peptides that discriminate full-length PrPSc from PrPC. Proc. Natl. Acad. Sci. USA 104: 11551-11556 [Abstract] [Full Text]  
  • Phuan, P.-W., Zorn, J. A., Safar, J., Giles, K., Prusiner, S. B., Cohen, F. E., May, B. C. H. (2007). Discriminating between cellular and misfolded prion protein by using affinity to 9-aminoacridine compounds. J. Gen. Virol. 88: 1392-1401 [Abstract] [Full Text]  
  • Legname, G., Nguyen, H.-O. B., Peretz, D., Cohen, F. E., DeArmond, S. J., Prusiner, S. B. (2006). Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc. Natl. Acad. Sci. USA 103: 19105-19110 [Abstract] [Full Text]  
  • Shiraishi, N., Utsunomiya, H., Nishikimi, M. (2006). Combination of NADPH and Copper Ions Generates Proteinase K-resistant Aggregates from Recombinant Prion Protein. J. Biol. Chem. 281: 34880-34887 [Abstract] [Full Text]  
  • Mathiason, C. K., Powers, J. G., Dahmes, S. J., Osborn, D. A., Miller, K. V., Warren, R. J., Mason, G. L., Hays, S. A., Hayes-Klug, J., Seelig, D. M., Wild, M. A., Wolfe, L. L., Spraker, T. R., Miller, M. W., Sigurdson, C. J., Telling, G. C., Hoover, E. A. (2006). Infectious prions in the saliva and blood of deer with chronic wasting disease.. Science 314: 133-136 [Abstract] [Full Text]  
  • Leliveld, S. R., Dame, R. T., Wuite, G. J. L., Stitz, L., Korth, C. (2006). The Expanded Octarepeat Domain Selectively Binds Prions and Disrupts Homomeric Prion Protein Interactions. J. Biol. Chem. 281: 3268-3275 [Abstract] [Full Text]  
  • Safar, J. G., DeArmond, S. J., Kociuba, K., Deering, C., Didorenko, S., Bouzamondo-Bernstein, E., Prusiner, S. B., Tremblay, P. (2005). Prion clearance in bigenic mice. J. Gen. Virol. 86: 2913-2923 [Abstract] [Full Text]  
  • Barron, R. M., Baybutt, H., Tuzi, N. L., McCormack, J., King, D., Moore, R. C., Melton, D. W., Manson, J. C. (2005). Polymorphisms at codons 108 and 189 in murine PrP play distinct roles in the control of scrapie incubation time. J. Gen. Virol. 86: 859-868 [Abstract] [Full Text]  
  • Legname, G., Nguyen, H.-O. B., Baskakov, I. V., Cohen, F. E., DeArmond, S. J., Prusiner, S. B. (2005). Strain-specified characteristics of mouse synthetic prions. Proc. Natl. Acad. Sci. USA 102: 2168-2173 [Abstract] [Full Text]  
  • Legname, G., Baskakov, I. V., Nguyen, H.-O. B., Riesner, D., Cohen, F. E., DeArmond, S. J., Prusiner, S. B. (2004). Synthetic Mammalian Prions. Science 305: 673-676 [Abstract] [Full Text]  
  • O'Rourke, K. I., Spraker, T. R., Hamburg, L. K., Besser, T. E., Brayton, K. A., Knowles, D. P. (2004). Polymorphisms in the prion precursor functional gene but not the pseudogene are associated with susceptibility to chronic wasting disease in white-tailed deer. J. Gen. Virol. 85: 1339-1346 [Abstract] [Full Text]  
  • Lawson, V. A., Priola, S. A., Meade-White, K., Lawson, M., Chesebro, B. (2004). Flexible N-terminal Region of Prion Protein Influences Conformation of Protease-resistant Prion Protein Isoforms Associated with Cross-species Scrapie Infection in Vivo and in Vitro. J. Biol. Chem. 279: 13689-13695 [Abstract] [Full Text]  
  • Barron, R. M., Thomson, V., King, D., Shaw, J., Melton, D. W., Manson, J. C. (2003). Transmission of murine scrapie to P101L transgenic mice. J. Gen. Virol. 84: 3165-3172 [Abstract] [Full Text]  
  • Satoh, K., Muramoto, T., Tanaka, T., Kitamoto, N., Ironside, J. W., Nagashima, K., Yamada, M., Sato, T., Mohri, S., Kitamoto, T. (2003). Association of an 11-12 kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt-Jakob disease and other prion diseases. J. Gen. Virol. 84: 2885-2893 [Abstract] [Full Text]  
  • Chiesa, R., Piccardo, P., Quaglio, E., Drisaldi, B., Si-Hoe, S. L., Takao, M., Ghetti, B., Harris, D. A. (2003). Molecular Distinction between Pathogenic and Infectious Properties of the Prion Protein. J. Virol. 77: 7611-7622 [Abstract] [Full Text]  
  • Korth, C., Kaneko, K., Groth, D., Heye, N., Telling, G., Mastrianni, J., Parchi, P., Gambetti, P., Will, R., Ironside, J., Heinrich, C., Tremblay, P., DeArmond, S. J., Prusiner, S. B. (2003). Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene. Proc. Natl. Acad. Sci. USA 100: 4784-4789 [Abstract] [Full Text]  
  • Vorberg, I., Groschup, M. H., Pfaff, E., Priola, S. A. (2003). Multiple Amino Acid Residues within the Rabbit Prion Protein Inhibit Formation of Its Abnormal Isoform. J. Virol. 77: 2003-2009 [Abstract] [Full Text]  
  • Legname, G., Nelken, P., Guan, Z., Kanyo, Z. F., DeArmond, S. J., Prusiner, S. B. (2002). Prion and doppel proteins bind to granule cells of the cerebellum. Proc. Natl. Acad. Sci. USA 99: 16285-16290 [Abstract] [Full Text]  
  • Perrier, V., Kaneko, K., Safar, J., Vergara, J., Tremblay, P., DeArmond, S. J., Cohen, F. E., Prusiner, S. B., Wallace, A. C. (2002). Dominant-negative inhibition of prion replication in transgenic mice. Proc. Natl. Acad. Sci. USA 99: 13079-13084 [Abstract] [Full Text]  
  • Warner, R. G., Hundt, C., Weiss, S., Turnbull, J. E. (2002). Identification of the Heparan Sulfate Binding Sites in the Cellular Prion Protein. J. Biol. Chem. 277: 18421-18430 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»