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Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

Author

Listed:
  • Nicholas K. Hurlburt

    (Vaccines and Infectious Diseases Division)

  • Emilie Seydoux

    (Vaccines and Infectious Diseases Division)

  • Yu-Hsin Wan

    (Vaccines and Infectious Diseases Division)

  • Venkata Viswanadh Edara

    (Emory University School of Medicine)

  • Andrew B. Stuart

    (Vaccines and Infectious Diseases Division)

  • Junli Feng

    (Vaccines and Infectious Diseases Division)

  • Mehul S. Suthar

    (Emory University School of Medicine)

  • Andrew T. McGuire

    (Vaccines and Infectious Diseases Division
    University of Washington)

  • Leonidas Stamatatos

    (Vaccines and Infectious Diseases Division
    University of Washington)

  • Marie Pancera

    (Vaccines and Infectious Diseases Division
    National Institute of Health)

Abstract

SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determine the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain. The structure reveals that CV30 binds to an epitope that overlaps with the human ACE2 receptor binding motif providing a structural basis for its neutralization. CV30 also induces shedding of the S1 subunit, indicating an additional mechanism of neutralization. A germline reversion of CV30 results in a substantial reduction in both binding affinity and neutralization potential indicating the minimal somatic mutation is needed for potently neutralizing antibodies against SARS-CoV-2.

Suggested Citation

  • Nicholas K. Hurlburt & Emilie Seydoux & Yu-Hsin Wan & Venkata Viswanadh Edara & Andrew B. Stuart & Junli Feng & Mehul S. Suthar & Andrew T. McGuire & Leonidas Stamatatos & Marie Pancera, 2020. "Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation," Nature Communications, Nature, vol. 11(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19231-9
    DOI: 10.1038/s41467-020-19231-9
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    Cited by:

    1. Haisheng Yu & Banghui Liu & Yudi Zhang & Xijie Gao & Qian Wang & Haitao Xiang & Xiaofang Peng & Caixia Xie & Yaping Wang & Peiyu Hu & Jingrong Shi & Quan Shi & Pingqian Zheng & Chengqian Feng & Guofan, 2023. "Somatically hypermutated antibodies isolated from SARS-CoV-2 Delta infected patients cross-neutralize heterologous variants," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Nathan Post & Danielle Eddy & Catherine Huntley & May C I van Schalkwyk & Madhumita Shrotri & David Leeman & Samuel Rigby & Sarah V Williams & William H Bermingham & Paul Kellam & John Maher & Adrian , 2020. "Antibody response to SARS-CoV-2 infection in humans: A systematic review," PLOS ONE, Public Library of Science, vol. 15(12), pages 1-27, December.

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