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IgGs are made for walking on bacterial and viral surfaces

Author

Listed:
  • Johannes Preiner

    (Center for Advanced Bioanalysis
    Institute of Biophysics, Johannes Kepler University Linz)

  • Noriyuki Kodera

    (Bio-AFM Frontier Research Center, Kanazawa University, Kakuma-machi)

  • Jilin Tang

    (Chang Chun Institute of Applied Chemistry, Chinese Academy Of Sciences)

  • Andreas Ebner

    (Institute of Biophysics, Johannes Kepler University Linz)

  • Mario Brameshuber

    (Institute of Applied Physics, Vienna University of Technology)

  • Dieter Blaas

    (Max F. Perutz Laboratories, Medical University of Vienna)

  • Nicola Gelbmann

    (University of Natural Resources and Applied Life Sciences Vienna
    Present address: Octapharma Pharmazeutika Produktionsges.m.b.H., Oberlaaer Strasse 235, A-1100 Vienna, Austria)

  • Hermann J. Gruber

    (Institute of Biophysics, Johannes Kepler University Linz)

  • Toshio Ando

    (Bio-AFM Frontier Research Center, Kanazawa University, Kakuma-machi
    Kanazawa University, Kakuma-machi)

  • Peter Hinterdorfer

    (Center for Advanced Bioanalysis
    Institute of Biophysics, Johannes Kepler University Linz)

Abstract

Binding of antibodies to their cognate antigens is fundamental for adaptive immunity. Molecular engineering of antibodies for therapeutic and diagnostic purposes emerges to be one of the major technologies in combating many human diseases. Despite its importance, a detailed description of the nanomechanical process of antibody–antigen binding and dissociation on the molecular level is lacking. Here we utilize high-speed atomic force microscopy to examine the dynamics of antibody recognition and uncover a principle; antibodies do not remain stationary on surfaces of regularly spaced epitopes; they rather exhibit ‘bipedal’ stochastic walking. As monovalent Fab fragments do not move, steric strain is identified as the origin of short-lived bivalent binding. Walking antibodies gather in transient clusters that might serve as docking sites for the complement system and/or phagocytes. Our findings could inspire the rational design of antibodies and multivalent receptors to exploit/inhibit steric strain-induced dynamic effects.

Suggested Citation

  • Johannes Preiner & Noriyuki Kodera & Jilin Tang & Andreas Ebner & Mario Brameshuber & Dieter Blaas & Nicola Gelbmann & Hermann J. Gruber & Toshio Ando & Peter Hinterdorfer, 2014. "IgGs are made for walking on bacterial and viral surfaces," Nature Communications, Nature, vol. 5(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5394
    DOI: 10.1038/ncomms5394
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    Cited by:

    1. Rong Zhu & Daniel Canena & Mateusz Sikora & Miriam Klausberger & Hannah Seferovic & Ahmad Reza Mehdipour & Lisa Hain & Elisabeth Laurent & Vanessa Monteil & Gerald Wirnsberger & Ralph Wieneke & Robert, 2022. "Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    2. Christoph Buhlheller & Theo Sagmeister & Christoph Grininger & Nina Gubensäk & Uwe B. Sleytr & Isabel Usón & Tea Pavkov-Keller, 2024. "SymProFold: Structural prediction of symmetrical biological assemblies," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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