This Article
Right arrow Full Text (PDF)
Right arrow An erratum has been published
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 Caughey, B
Right arrow Articles by Thresher, W
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Caughey, B
Right arrow Articles by Thresher, W

 Previous Article  |  Next Article 

J Virol. 1994 April; 68(4): 2135-2141

Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]

B Caughey, K Brown, G J Raymond, G E Katzenstein and W Thresher

Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, Hamilton, Montana 59840.

ABSTRACT

Congo red and certain sulfated glycans are potent inhibitors of protease-resistant PrP accumulation in scrapie-infected cells. One hypothesis is that these inhibitors act by blocking the association between protease-resistant PrP and sulfated glycosaminoglycans or proteoglycans (e.g., heparan sulfate proteoglycan) that is observed in amyloid plaques of scrapie-infected brain tissue. Accordingly, we have investigated whether the apparent precursor of protease-resistant PrP, protease-sensitive PrP, binds to Congo red and heparin, a highly sulfated glycosaminoglycan with an inhibitory potency like that of heparan sulfate. Protease-sensitive PrP released from the surface of mouse neuroblastoma cells bound to heparin-agarose and Congo red-glass beads. Sucrose density gradient fractionation provided evidence that at least some of the PrP capable of binding heparin-agarose was monomeric. Free Congo red blocked PrP binding to heparin and vice versa, suggesting that these ligands share a common binding site. The relative efficacies of pentosan polysulfate, Congo red, heparin, and chondroitin sulfate in blocking PrP binding to heparin-agarose corresponded with their previously demonstrated potencies in inhibiting protease-resistant PrP accumulation. These results are consistent with the idea that sulfated glycans and Congo red inhibit protease-resistant PrP accumulation by interfering with the interaction of PrP with an endogenous glycosaminoglycan or proteoglycan.

J Virol. 1994 April; 68(4): 2135-2141




This article has been cited by other articles:

  • Elimova, E., Kisilevsky, R., Ancsin, J. B. (2009). Heparan sulfate promotes the aggregation of HDL-associated serum amyloid A: evidence for a proamyloidogenic histidine molecular switch. FASEB J. 23: 3436-3448 [Abstract] [Full Text]  
  • CORATO, M., OGLIARI, P., CECILIANI, F., COVA, E., BELLOTTI, V., CEREDA, C., MERLINI, G., CERONI, M. (2009). Doxorubicin and Congo Red Effectiveness on Prion Infectivity in Golden Syrian Hamster. Anticancer Res 29: 2507-2512 [Abstract] [Full Text]  
  • Gomes, M. P. B., Millen, T. A., Ferreira, P. S., e Silva, N. L. C., Vieira, T. C. R. G., Almeida, M. S., Silva, J. L., Cordeiro, Y. (2008). Prion Protein Complexed to N2a Cellular RNAs through Its N-terminal Domain Forms Aggregates and Is Toxic to Murine Neuroblastoma Cells. J. Biol. Chem. 283: 19616-19625 [Abstract] [Full Text]  
  • Mahal, S. P., Baker, C. A., Demczyk, C. A., Smith, E. W., Julius, C., Weissmann, C. (2007). Prion strain discrimination in cell culture: The cell panel assay. Proc. Natl. Acad. Sci. USA 104: 20908-20913 [Abstract] [Full Text]  
  • Geoghegan, J. C., Valdes, P. A., Orem, N. R., Deleault, N. R., Williamson, R. A., Harris, B. T., Supattapone, S. (2007). Selective Incorporation of Polyanionic Molecules into Hamster Prions. J. Biol. Chem. 282: 36341-36353 [Abstract] [Full Text]  
  • Trevitt, C. R, Collinge, J. (2006). A systematic review of prion therapeutics in experimental models. Brain 129: 2241-2265 [Abstract] [Full Text]  
  • Kocisko, D. A., Vaillant, A., Lee, K. S., Arnold, K. M., Bertholet, N., Race, R. E., Olsen, E. A., Juteau, J.-M., Caughey, B. (2006). Potent Antiscrapie Activities of Degenerate Phosphorothioate Oligonucleotides. Antimicrob. Agents Chemother. 50: 1034-1044 [Abstract] [Full Text]  
  • Sekiya, S., Noda, K., Nishikawa, F., Yokoyama, T., Kumar, P. K.R., Nishikawa, S. (2006). Characterization and Application of a Novel RNA Aptamer against the Mouse Prion Protein.. J Biochem 139: 383-390 [Abstract] [Full Text]  
  • Nordstrom, E. K., Luhr, K. M., Ibanez, C., Kristensson, K. (2005). Inhibitors of the Mitogen-Activated Protein Kinase Kinase 1/2 Signaling Pathway Clear Prion-Infected Cells from PrPSc. J. Neurosci. 25: 8451-8456 [Abstract] [Full Text]  
  • Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Favara, C., Baron, G., Priola, S., Caughey, B., Masliah, E., Oldstone, M. (2005). Anchorless Prion Protein Results in Infectious Amyloid Disease Without Clinical Scrapie. Science 308: 1435-1439 [Abstract] [Full Text]  
  • Novakofski, J., Brewer, M. S., Mateus-Pinilla, N., Killefer, J., McCusker, R. H. (2005). Prion biology relevant to bovine spongiform encephalopathy. J ANIM SCI 83: 1455-1476 [Abstract] [Full Text]  
  • Horonchik, L., Tzaban, S., Ben-Zaken, O., Yedidia, Y., Rouvinski, A., Papy-Garcia, D., Barritault, D., Vlodavsky, I., Taraboulos, A. (2005). Heparan Sulfate Is a Cellular Receptor for Purified Infectious Prions. J. Biol. Chem. 280: 17062-17067 [Abstract] [Full Text]  
  • Jones, L. S., Yazzie, B., Middaugh, C. R. (2004). Polyanions and the Proteome. Mol. Cell. Proteomics 3: 746-769 [Abstract] [Full Text]  
  • Doh-ura, K., Ishikawa, K., Murakami-Kubo, I., Sasaki, K., Mohri, S., Race, R., Iwaki, T. (2004). Treatment of Transmissible Spongiform Encephalopathy by Intraventricular Drug Infusion in Animal Models. J. Virol. 78: 4999-5006 [Abstract] [Full Text]  
  • Luhr, K. M., Nordstrom, E. K., Low, P., Ljunggren, H.-G., Taraboulos, A., Kristensson, K. (2004). Scrapie Protein Degradation by Cysteine Proteases in CD11c+ Dendritic Cells and GT1-1 Neuronal Cells. J. Virol. 78: 4776-4782 [Abstract] [Full Text]  
  • Nakamura, Y., Sakudo, A., Saeki, K., Kaneko, T., Matsumoto, Y., Toniolo, A., Itohara, S., Onodera, T. (2003). Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells. J. Gen. Virol. 84: 3495-3502 [Abstract] [Full Text]  
  • Rhie, A., Kirby, L., Sayer, N., Wellesley, R., Disterer, P., Sylvester, I., Gill, A., Hope, J., James, W., Tahiri-Alaoui, A. (2003). Characterization of 2'-Fluoro-RNA Aptamers That Bind Preferentially to Disease-associated Conformations of Prion Protein and Inhibit Conversion. J. Biol. Chem. 278: 39697-39705 [Abstract] [Full Text]  
  • Ben-Zaken, O., Tzaban, S., Tal, Y., Horonchik, L., Esko, J. D., Vlodavsky, I., Taraboulos, A. (2003). Cellular Heparan Sulfate Participates in the Metabolism of Prions. J. Biol. Chem. 278: 40041-40049 [Abstract] [Full Text]  
  • Aguzzi, A., Hardt, W.-D. (2003). Dangerous Liaisons between a Microbe and the Prion Protein. JEM 198: 1-4 [Full Text]  
  • Lasmezas, C. I. (2003). Putative functions of PrPC. Br Med Bull 66: 61-70 [Abstract] [Full Text]  
  • Kim, Y.-S., Randolph, T. W., Manning, M. C., Stevens, F. J., Carpenter, J. F. (2003). Congo Red Populates Partially Unfolded States of an Amyloidogenic Protein to Enhance Aggregation and Amyloid Fibril Formation. J. Biol. Chem. 278: 10842-10850 [Abstract] [Full Text]  
  • Marella, M., Lehmann, S., Grassi, J., Chabry, J. (2002). Filipin Prevents Pathological Prion Protein Accumulation by Reducing Endocytosis and Inducing Cellular PrP Release. J. Biol. Chem. 277: 25457-25464 [Abstract] [Full Text]  
  • Brown, P. (2002). Drug therapy in human and experimental transmissible spongiform encephalopathy. Neurology 58: 1720-1725 [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]  
  • 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 [Abstract] [Full Text]  
  • Mangé, A., Nishida, N., Milhavet, O., McMahon, H. E. M., Casanova, D., Lehmann, S. (2000). Amphotericin B Inhibits the Generation of the Scrapie Isoform of the Prion Protein in Infected Cultures. J. Virol. 74: 3135-3140 [Abstract] [Full Text]  
  • Rudyk, H., Vasiljevic, S., Hennion, R. M., Birkett, C. R., Hope, J., Gilbert, I. H. (2000). Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. J. Gen. Virol. 81: 1155-1164 [Abstract] [Full Text]  
  • Nishida, N., Harris, D. A., Vilette, D., Laude, H., Frobert, Y., Grassi, J., Casanova, D., Milhavet, O., Lehmann, S. (2000). Successful Transmission of Three Mouse-Adapted Scrapie Strains to Murine Neuroblastoma Cell Lines Overexpressing Wild-Type Mouse Prion Protein. J. Virol. 74: 320-325 [Abstract] [Full Text]  
  • Supattapone, S., Nguyen, H.-O. B., Cohen, F. E., Prusiner, S. B., Scott, M. R. (1999). Elimination of prions by branched polyamines and implications for therapeutics. Proc. Natl. Acad. Sci. USA 96: 14529-14534 [Abstract] [Full Text]  
  • Ancsin, J. B., Kisilevsky, R. (1999). The Heparin/Heparan Sulfate-binding Site on Apo-serum Amyloid A. IMPLICATIONS FOR THE THERAPEUTIC INTERVENTION OF AMYLOIDOSIS. J. Biol. Chem. 274: 7172-7181 [Abstract] [Full Text]  
  • DebBurman, S. K., Raymond, G. J., Caughey, B., Lindquist, S. (1997). Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA 94: 13938-13943 [Abstract] [Full Text]  
  • Shyng, S.-L., Lehmann, S., Moulder, K. L., Harris, D. A. (1995). Sulfated Glycans Stimulate Endocytosis of the Cellular Isoform of the Prion Protein, PrP^C, in Cultured Cells. J. Biol. Chem. 270: 30221-30229 [Abstract] [Full Text]  
  • Lehmann, S., Harris, D. A. (1995). A Mutant Prion Protein Displays an Aberrant Membrane Association When Expressed in Cultured Cells. J. Biol. Chem. 270: 24589-24597 [Abstract] [Full Text]  
  • Chen, S. G., Teplow, D. B., Parchi, P., Teller, J. K., Gambetti, P., Autilio-Gambetti, L. (1995). Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases. J. Biol. Chem. 270: 19173-19180 [Abstract] [Full Text]  
  • Shaked, G. M., Meiner, Z., Avraham, I., Taraboulos, A., Gabizon, R. (2001). Reconstitution of Prion Infectivity from Solubilized Protease-resistant PrP and Nonprotein Components of Prion Rods. J. Biol. Chem. 276: 14324-14328 [Abstract] [Full Text]  
  • Gabus, C., Derrington, E., Leblanc, P., Chnaiderman, J., Dormont, D., Swietnicki, W., Morillas, M., Surewicz, W. K., Marc, D., Nandi, P., Darlix, J.-L. (2001). The Prion Protein Has RNA Binding and Chaperoning Properties Characteristic of Nucleocapsid Protein NCp7 of HIV-1. J. Biol. Chem. 276: 19301-19309 [Abstract] [Full Text]  
  • Khurana, R., Uversky, V. N., Nielsen, L., Fink, A. L. (2001). Is Congo Red an Amyloid-specific Dye?. J. Biol. Chem. 276: 22715-22721 [Abstract] [Full Text]  
  • Cordeiro, Y., Machado, F., Juliano, L., Juliano, M. A., Brentani, R. R., Foguel, D., Silva, J. L. (2001). DNA Converts Cellular Prion Protein into the beta -Sheet Conformation and Inhibits Prion Peptide Aggregation. J. Biol. Chem. 276: 49400-49409 [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»