Unraveling the Dynamics of Antibody-Antigen Interaction by DNA Origami
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doi: 10.1007/s40242-020-0252-6
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Unraveling the Dynamics of Antibody-Antigen Interaction by DNA Origami NIE Zhou* State Key Laboratory of Chemo/Bio-sensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan Provincial Key Laboratory of Biomacromolecular Chemical Biology, Hunan University, Changsha 410082, P. R. China Abstract To investigate the dynamic interaction between antibody and antigen, Fan et al. rationally designed a triangular DNA origami framework to spatially organize the antigenic epitopes at the nanoscale and thus to monitor the transient binding kinetics of the dynamic antigen-antibody complexes at room temperature. This study provides a straightforward, designable and programmable strategy to investigate the transition kinetics of antibody-antigen interaction at a single-molecule level and improve the understanding toward the design of the next-generation antibodies and vaccines for various biomedical applications. This work has been published online in Nature Communications on June 19, 2020. The recognition of pathogenic antigens by antibodies is an important natural defense strategy in the mammalian adaptive immune system[1]. The avidity of the antibody is mainly determined by the antibody structure and the spatial presentation of antigenic epitopes on the surface of a viral particle[2]. However, it remains difficult to explore the dynamic anti-body-antigen interaction with high spatiotemporal resolution. Recently, Fan et al.[3] have developed an elegant DNA origami-based strategy to probe the transient binding of the antibody to the antigen at a
Fig.1
single-molecular level. Exploiting the excellent addressability and programmability of DNA self-assembly, the authors successfully fabricated a triangular DNA origami framework to spatially organize the artificial epitopes at the nanoscale, namely, DNA origami epitopes(DOEs). The designed DOEs site-specifically anchored six pairs of artificial epitope molecules on the prescribed positions with tailored lateral distances between each epitope pair, ranging from 3 nm to 20 nm [Fig.1(A)]. The rigidity of DOEs allows room-temperature
Schematic illustration of epitope spikes on the surface of a viral particle and DOEs for IgG capture and binding(A), peak force-AFM image for DOEs-captured IgGs(B), schematic of the three-stage binding process(left) and corresponding HS-AFM images(right)(C), and distinct conformations of single IgG captured by DOEs with designed distances, and schematic illustration(left) and snapshot HS-AFM images(right)(D)[3] (B) Scale bar, 20 nm; (C) scale bar, 10 nm; (D) scale bar, 10 nm.
——————————— *Corresponding author. Email: [email protected] Received August 4, 2020; accepted August 7, 2020. © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH
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Chem. Res. Chinese Universities
freezing of captured immunoglobin G proteins(IgG) for highresolution imaging of transient binding conformations. Using atomic force microscopy(AFM), they il
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