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Antibodies inhibit prion propagation and clear cell cultures of prion infectivity

Academic Article
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Overview

authors

  • Peretz, D.
  • Williamson, R. A.
  • Kaneko, K.
  • Vergara, J.
  • Leclerc, E.
  • Schmitt-Ulms, G.
  • Mehlhorn, I. R.
  • Legname, G.
  • Wormald, M. R.
  • Rudd, P. M.
  • Dwek, R. A.
  • Burton, Dennis
  • Prusiner, S. B.

publication date

  • August 2001

journal

  • Nature  Journal

abstract

  • Prions are the transmissible pathogenic agents responsible for diseases such as scrapie and bovine spongiform encephalopathy. In the favoured model of prion replication, direct interaction between the pathogenic prion protein (PrPSc) template and endogenous cellular prion protein (PrPC) is proposed to drive the formation of nascent infectious prions. Reagents specifically binding either prion-protein conformer may interrupt prion production by inhibiting this interaction. We examined the ability of several recombinant antibody antigen-binding fragments (Fabs) to inhibit prion propagation in cultured mouse neuroblastoma cells (ScN2a) infected with PrPSc. Here we show that antibodies binding cell-surface PrPC inhibit PrPSc formation in a dose-dependent manner. In cells treated with the most potent antibody, Fab D18, prion replication is abolished and pre-existing PrPSc is rapidly cleared, suggesting that this antibody may cure established infection. The potent activity of Fab D18 is associated with its ability to better recognize the total population of PrPC molecules on the cell surface, and with the location of its epitope on PrPC. Our observations support the use of antibodies in the prevention and treatment of prion diseases and identify a region of PrPC for drug targeting.

subject areas

  • Animals
  • Antibody Specificity
  • Biological Assay
  • Epitopes, B-Lymphocyte
  • Escherichia coli
  • Immunoglobulin Fragments
  • Mice
  • PrPC Proteins
  • Prions
  • Recombinant Proteins
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/35089090

PubMed ID

  • 11507642
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Additional Document Info

start page

  • 739

end page

  • 743

volume

  • 412

issue

  • 6848

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