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BIOPHYSICS

Great stretches for your antibody workout

Nature Nanotechnology volume 14, pages 101–102 (2019)Cite this article

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DNA origami unravels the role of target spacing in antibody binding.

Multivalency is ubiquitous in biology. Proteins in living organisms hold together through multiple weak interactions, creating dynamic, yet stable complexes. Antibodies are a good example. Each antibody carries two binding sites for antigens, and their simultaneous engagement is critical for strong binding, clearing of pathogens and efficacy in therapy. However, the exact benefits of bivalent binding, called avidity, have been difficult to predict across different antibodies. This is because avidity depends both on the antibody structure and on the spacing and orientation of the antigens on the target, such a viral particle or a diseased cell1,2. In Nature Nanotechnology3, Shaw et al. use DNA origami to develop an elegant system to precisely control antigen spacing and thus establish its effects on antibody avidity. The results open new avenues to engineer antibodies that can engage better with multivalent targets.

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Fig. 1: DNA origami.

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Authors and Affiliations

  1. Immune Receptor Activation Laboratory, The Francis Crick Institute, London, UK

    Pavel Tolar

  2. Division of Immunology and Inflammation, Imperial College London, London, UK

    Pavel Tolar

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  1. Pavel Tolar
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Correspondence to Pavel Tolar.

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Tolar, P. Great stretches for your antibody workout. Nature Nanotech 14, 101–102 (2019). https://doi.org/10.1038/s41565-018-0354-1

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  • DOI: https://doi.org/10.1038/s41565-018-0354-1

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