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Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain

Author

Listed:
  • Timothy J. C. Tan

    (University of Illinois at Urbana-Champaign)

  • Meng Yuan

    (The Scripps Research Institute)

  • Kaylee Kuzelka

    (University of Illinois at Urbana-Champaign)

  • Gilberto C. Padron

    (University of Illinois at Urbana-Champaign)

  • Jacob R. Beal

    (University of Illinois at Urbana-Champaign)

  • Xin Chen

    (University of Illinois at Urbana-Champaign)

  • Yiquan Wang

    (University of Illinois at Urbana-Champaign)

  • Joel Rivera-Cardona

    (University of Illinois at Urbana-Champaign)

  • Xueyong Zhu

    (The Scripps Research Institute)

  • Beth M. Stadtmueller

    (University of Illinois at Urbana-Champaign)

  • Christopher B. Brooke

    (University of Illinois at Urbana-Champaign
    University of Illinois at Urbana-Champaign)

  • Ian A. Wilson

    (The Scripps Research Institute
    The Scripps Research Institute
    IAVI Neutralizing Antibody Center, The Scripps Research Institute
    The Scripps Research Institute)

  • Nicholas C. Wu

    (University of Illinois at Urbana-Champaign
    University of Illinois at Urbana-Champaign
    University of Illinois at Urbana-Champaign)

Abstract

Since the COVID-19 pandemic onset, the antibody response to SARS-CoV-2 has been extensively characterized. Antibodies to the receptor binding domain (RBD) on the spike protein are frequently encoded by IGHV3-53/3-66 with a short complementarity-determining region (CDR) H3. Germline-encoded sequence motifs in heavy chain CDRs H1 and H2 have a major function, but whether any common motifs are present in CDR H3, which is often critical for binding specificity, is not clear. Here, we identify two public clonotypes of IGHV3-53/3-66 RBD antibodies with a 9-residue CDR H3 that pair with different light chains. Distinct sequence motifs on CDR H3 are present in the two public clonotypes that seem to be related to differential light chain pairing. Additionally, we show that Y58F is a common somatic hypermutation that results in increased binding affinity of IGHV3-53/3-66 RBD antibodies with a short CDR H3. These results advance understanding of the antibody response to SARS-CoV-2.

Suggested Citation

  • Timothy J. C. Tan & Meng Yuan & Kaylee Kuzelka & Gilberto C. Padron & Jacob R. Beal & Xin Chen & Yiquan Wang & Joel Rivera-Cardona & Xueyong Zhu & Beth M. Stadtmueller & Christopher B. Brooke & Ian A., 2021. "Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24123-7
    DOI: 10.1038/s41467-021-24123-7
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