You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Characterization of Anti-Anti-Idiotypic Antibodies that Bind Antigen and an Anti-Idiotype
Fernando A. Goldbaum, C. Alejandro Velikovsky, William Dall'Acqua, Carlos A. Fossati, Barry A. Fields, Bradford C. Braden, Roberto J. Poljak and Roy A. Mariuzza
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 16 (Aug. 5, 1997), pp. 8697-8701
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/42920
Page Count: 5
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Two mouse monoclonal anti-anti-idiotopic antibodies (anti-anti-Id, Ab3), AF14 and AF52, were prepared by immunizing BALB/c mice with rabbit polyclonal anti-idiotypic antibodies (anti-Id, Ab2) raised against antibody D1.3 (Ab1) specific for the antigen hen egg lysozyme. AF14 and AF52 react with an ``internal image'' monoclonal mouse anti-Id antibody E5.2 (Ab2), previously raised against D1.3, with affinity constants (1.0 × 109 M-1 and 2.4 × 107 M-1, respectively) usually observed in secondary responses against protein antigens. They also react with the antigen but with lower affinity (1.8 × 106 M-1 and 3.8 × 106 M-1). This pattern of affinities for the anti-Id and for the antigen also was displayed by the sera of the immunized mice. The amino acid sequences of AF14 and AF52 are very close to that of D1.3. In particular, the amino acid side chains that contribute to contacts with both antigen and anti-Id are largely conserved in AF14 and AF52 compared with D1.3. Therapeutic immunizations against different pathogenic antigens using anti-Id antibodies have been proposed. Our experiments show that a response to an anti-Id immunogen elicits anti-anti-Id antibodies that are optimized for binding the anti-Id antibodies rather than the antigen.
Proceedings of the National Academy of Sciences of the United States of America © 1997 National Academy of Sciences