IgGs are made for walking on bacterial and viral surfaces

Johannes Preiner, Noriyuki Kodera, Jilin Tang, Andreas Ebner, Mario Brameshuber, Dieter Blaas, Nicola Gelbmann, Hermann J. Gruber, Toshio Ando and Peter Hinterdorfer ()
Additional contact information
Johannes Preiner: Center for Advanced Bioanalysis
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
Hermann J. Gruber: Institute of Biophysics, Johannes Kepler University Linz
Toshio Ando: Bio-AFM Frontier Research Center, Kanazawa University, Kakuma-machi
Peter Hinterdorfer: Center for Advanced Bioanalysis

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5394

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