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Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences

William F. Dall’ Acqua, Robert M. Woods, E. Sally Ward, Susan R. Palaszynski, Nita K. Patel, Yambasu A. Brewah, Herren Wu, Peter A. Kiener and Solomon Langermann
J Immunol November 1, 2002, 169 (9) 5171-5180; DOI: https://doi.org/10.4049/jimmunol.169.9.5171
William F. Dall’ Acqua
*MedImmune, Gaithersburg, MD 20878; and
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Robert M. Woods
*MedImmune, Gaithersburg, MD 20878; and
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E. Sally Ward
†Center for Immunology and Cancer Immunobiology Center, University of Texas Southwestern Medical Center, Dallas, TX 75390
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Susan R. Palaszynski
*MedImmune, Gaithersburg, MD 20878; and
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Nita K. Patel
*MedImmune, Gaithersburg, MD 20878; and
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Yambasu A. Brewah
*MedImmune, Gaithersburg, MD 20878; and
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Herren Wu
*MedImmune, Gaithersburg, MD 20878; and
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Peter A. Kiener
*MedImmune, Gaithersburg, MD 20878; and
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Solomon Langermann
*MedImmune, Gaithersburg, MD 20878; and
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Abstract

Many biological functions, including control of the homeostasis and maternofetal transfer of serum γ-globulins, are mediated by the MHC class I-related neonatal FcR (FcRn). A correlation exists in mice between the binding affinity of IgG1/Fc fragments to FcRn at pH 6.0 and their serum t1/2. To expand this observation, phage display of mutagenized Fc fragments derived from a human IgG1 was used to increase their affinity to both murine and human FcRn. Ten variants were identified that have a higher affinity toward murine and human FcRn at pH 6.0, with ΔΔG (ΔGwild type − ΔGmutant) from 1.0 to 2.0 kcal/mol and from 0.6 to 2.4 kcal/mol, respectively. Those variants exhibit a parallel increase in binding at pH 7.4 to murine, but not human, FcRn. Although not degraded in blood in vitro, accumulated in tissues, nor excreted in urine, their serum concentration in mice is decreased. We propose that higher affinity to FcRn at pH 7.4 adversely affects release into the serum and offsets the benefit of the enhanced binding at pH 6.0.

  • Received June 25, 2002.
  • Accepted September 3, 2002.
  • Copyright © 2002 by The American Association of Immunologists
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The Journal of Immunology: 169 (9)
The Journal of Immunology
Vol. 169, Issue 9
1 Nov 2002
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Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences
William F. Dall’ Acqua, Robert M. Woods, E. Sally Ward, Susan R. Palaszynski, Nita K. Patel, Yambasu A. Brewah, Herren Wu, Peter A. Kiener, Solomon Langermann
The Journal of Immunology November 1, 2002, 169 (9) 5171-5180; DOI: 10.4049/jimmunol.169.9.5171

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Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences
William F. Dall’ Acqua, Robert M. Woods, E. Sally Ward, Susan R. Palaszynski, Nita K. Patel, Yambasu A. Brewah, Herren Wu, Peter A. Kiener, Solomon Langermann
The Journal of Immunology November 1, 2002, 169 (9) 5171-5180; DOI: 10.4049/jimmunol.169.9.5171
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