Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein
| Autor: | David Peretz, Hana Serban, Dennis R. Burton, Stephen J. DeArmond, Nechama I. Smorodinsky, Stanley B. Prusiner, Ingrid Mehlhorn, R A Williamson, Raiza Bastidas |
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| Rok vydání: | 1996 |
| Předmět: |
Phage display
Prions medicine.drug_class animal diseases Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Biology Monoclonal antibody Polymerase Chain Reaction Prion Diseases Immune tolerance law.invention PRNP Immunoglobulin Fab Fragments Mice Immune system Protein structure Antibody Specificity law Cricetinae Immune Tolerance medicine Animals DNA Primers Multidisciplinary Base Sequence Mesocricetus Antibodies Monoclonal Virology Molecular biology Recombinant Proteins nervous system diseases biology.protein Recombinant DNA Antibody Immunoglobulin Heavy Chains Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 93:7279-7282 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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