Designed proteins assemble antibodies into modular nanocages

  • Robby Divine
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Ha V. Dang
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • George Ueda
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Jorge A. Fallas
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Ivan Vulovic
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • William Sheffler
    Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Shally Saini
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Yan Ting Zhao
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Infencia Xavier Raj
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Peter A. Morawski
    Benaroya Research Institute, Seattle, WA 98101, USA.
  • Madeleine F. Jennewein
    Vaccines and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98019, USA.
  • Leah J. Homad
    Vaccines and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98019, USA.
  • Yu-Hsin Wan
    Vaccines and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98019, USA.
  • Marti R. Tooley
    Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Franziska Seeger
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Ali Etemadi
    Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Mitchell L. Fahning
    Benaroya Research Institute, Seattle, WA 98101, USA.
  • James Lazarovits
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Alex Roederer
    Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Alexandra C. Walls
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Lance Stewart
    Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
  • Mohammadali Mazloomi
    Medical Biotechnology Department, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences (TUMS), Tehran, Iran.
  • Neil P. King
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Daniel J. Campbell
    Benaroya Research Institute, Seattle, WA 98101, USA.
  • Andrew T. McGuire
    Vaccines and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98019, USA.
  • Leonidas Stamatatos
    Vaccines and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98019, USA.
  • Hannele Ruohola-Baker
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Julie Mathieu
    Institute for Stem Cell and Regenerative Medicine, University of Washington, Seattle, WA 98109, USA.
  • David Veesler
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • David Baker
    Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.

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<jats:title>Integrating form and function for design</jats:title> <jats:p> Antibodies are broadly used in therapies and as research tools because they can be generated against a wide range of targets. Efficacy can often be increased by clustering antibodies in multivalent assemblies. Divine <jats:italic>et al.</jats:italic> designed antibody nanocages from two components: One is an antibody-binding homo-oligomic protein and the other is the antibody itself. Computationally designed proteins drive the assembly of antibody nanocages in a range of architectures, allowing control of the symmetry and the antibody valency. The multivalent display enhances antibody-dependent signaling, and nanocages displaying antibodies against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein effectively neutralize pseudovirus. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" related-article-type="in-this-issue" xlink:href="10.1126/science.abd9994">eabd9994</jats:related-article> </jats:p>

収録刊行物

  • Science

    Science 372 (6537), eabd9994-, 2021-04-02

    American Association for the Advancement of Science (AAAS)

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