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Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation

Author

Listed:
  • Hugo Mouquet

    (Laboratory of Molecular Immunology, The Rockefeller University)

  • Johannes F. Scheid

    (Laboratory of Molecular Immunology, The Rockefeller University
    Charite Universitaetsmedizin)

  • Markus J. Zoller

    (Max Planck Institute for Infection Biology)

  • Michelle Krogsgaard

    (New York University School of Medicine)

  • Rene G. Ott

    (Laboratory of Molecular Genetics and Immunology, The Rockefeller University)

  • Shetha Shukair

    (Northwestern University)

  • Maxim N. Artyomov

    (Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology)

  • John Pietzsch

    (Laboratory of Molecular Immunology, The Rockefeller University
    Institute of Chemistry and Biochemistry, Freie Universität Berlin)

  • Mark Connors

    (Laboratory of Immunoregulation, and Vaccine Research Center, National Institutes of Allergy and Infectious Diseases, National Institutes of Health)

  • Florencia Pereyra

    (Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School)

  • Bruce D. Walker

    (Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology and Harvard Medical School)

  • David D. Ho

    (Aaron Diamond AIDS Research Center)

  • Patrick C. Wilson

    (Section of Rheumatology, University of Chicago)

  • Michael S. Seaman

    (Beth Israel Deaconess Medical Center)

  • Herman N. Eisen

    (Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology)

  • Arup K. Chakraborty

    (Chemical Engineering, Biology, and Biological Engineering, and Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology)

  • Thomas J. Hope

    (Northwestern University)

  • Jeffrey V. Ravetch

    (Laboratory of Molecular Genetics and Immunology, The Rockefeller University)

  • Hedda Wardemann

    (Max Planck Institute for Infection Biology)

  • Michel C. Nussenzweig

    (Laboratory of Molecular Immunology, The Rockefeller University
    Howard Hughes Medical Institute, The Rockefeller University)

Abstract

Antibodies hedge their bets Most antibodies are highly specific, binding with high affinity to a single foreign antigen. However, an analysis of human immunodeficiency virus (HIV) envelope glycoprotein-specific monoclonal antibodies from infected subjects provides evidence for a surprisingly high degree of polyreactivity. Of 134 different antibodies directed at the gp140 envelope glycoprotein cloned from six patients, 75% were polyreactive, binding with high affinity to one gp140 site and with lower affinity to other sites on the viral surface. Relatively few gp140 glycoprotein spikes are displayed on the surface of HIV, so homotypic bivalent antibody binding is disfavoured and 'heteroligation' may help to improve net antibody affinity in such instances.

Suggested Citation

  • Hugo Mouquet & Johannes F. Scheid & Markus J. Zoller & Michelle Krogsgaard & Rene G. Ott & Shetha Shukair & Maxim N. Artyomov & John Pietzsch & Mark Connors & Florencia Pereyra & Bruce D. Walker & Dav, 2010. "Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation," Nature, Nature, vol. 467(7315), pages 591-595, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7315:d:10.1038_nature09385
    DOI: 10.1038/nature09385
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    Cited by:

    1. Edward P. Harvey & Jung-Eun Shin & Meredith A. Skiba & Genevieve R. Nemeth & Joseph D. Hurley & Alon Wellner & Ada Y. Shaw & Victor G. Miranda & Joseph K. Min & Chang C. Liu & Debora S. Marks & Andrew, 2022. "An in silico method to assess antibody fragment polyreactivity," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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