NR AMPQ
AU Williamson,R.A.; Peretz,D.; Smorodinsky,N.; Bastidas,R.B.; Serban,H.; Mehlhorn,I.; DeArmond,S.J.; Prusiner,S.B.; Burton,D.R.
TI Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein
QU Proceedings of the National Academy of Sciences of the United States of America 1996 Jul 9; 93(14): 7279-82
PT journal article
AB 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.
ZR 41
MH Animal; Antibodies, Monoclonal/*biosynthesis; Antibody Specificity; Base Sequence; DNA Primers; Enzyme-Linked Immunosorbent Assay; Hamsters; *Immune Tolerance; Immunoglobulins, Fab/biosynthesis; Immunoglobulins, Heavy-Chain/biosynthesis; Mesocricetus; Mice; Molecular Sequence Data; Polymerase Chain Reaction; Prion Diseases/*immunology; Prions/analysis/*immunology; Recombinant Proteins/biosynthesis; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA
SP englisch
PO USA