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Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein

Academic Article
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Overview

authors

  • Williamson, R. A.
  • Peretz, D.
  • Smorodinsky, N.
  • Bastidas, R.
  • Serban, H.
  • Mehlhorn, I.
  • DeArmond, S. J.
  • Prusiner, S. B.
  • Burton, Dennis

publication date

  • 1996

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Prion diseases are disorders of protein conformation and do not provoke an immune response. Raising antibodies to the prion protein (PrP) has been difficult due to conservation of the PrP sequence and to inhibitory activity of alpha-PrP antibodies toward lymphocytes. To circumvent these problems, we immunized mice in which the PrP gene was ablated (Prnp 0/0) and retrieved specific monoclonal antibodies (mAbs) through phage display libraries. This approach yielded alpha-PrP mAbs that recognize mouse PrP. Studies with these mAbs suggest that cellular PrP adopts an unusually open structure consistent with the conformational plasticity of this protein.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antibody Specificity
  • Base Sequence
  • Cricetinae
  • DNA Primers
  • Enzyme-Linked Immunosorbent Assay
  • Immune Tolerance
  • Immunoglobulin Fab Fragments
  • Immunoglobulin Heavy Chains
  • Mesocricetus
  • Mice
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Prion Diseases
  • Prions
  • Recombinant Proteins
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Research

keywords

  • gene ablation
  • mouse antibody libraries
  • phage display
  • prion disease
  • scrapie
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Identity

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.93.14.7279

PubMed ID

  • 8692983
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Additional Document Info

start page

  • 7279

end page

  • 7282

volume

  • 93

issue

  • 14

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