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Jeong BS, Cha JS, Hwang I, et al. Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants. MAbs. 2022;14(1):2021601doi: 10.1080/19420862.2021.2021601.
Jeong, B. S., Cha, J. S., Hwang, I., Kim, U., Adolf-Bryfogle, J., Coventry, B., Cho, H. S., Kim, K. D., & Oh, B. H. (2022). Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants. mAbs, 14(1), 2021601. https://doi.org/10.1080/19420862.2021.2021601
Jeong, Bo-Seong, et al. "Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants." mAbs vol. 14,1 (2022): 2021601. doi: https://doi.org/10.1080/19420862.2021.2021601
Jeong BS, Cha JS, Hwang I, Kim U, Adolf-Bryfogle J, Coventry B, Cho HS, Kim KD, Oh BH. Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants. MAbs. 2022 Jan-Dec;14(1):2021601. doi: 10.1080/19420862.2021.2021601. PMID: 35030983.
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MAbs. 2022 Jan-Dec;14(1):2021601. doi: 10.1080/19420862.2021.2021601.

Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants.

mAbs

Bo-Seong Jeong, Jeong Seok Cha, Insu Hwang, Uijin Kim, Jared Adolf-Bryfogle, Brian Coventry, Hyun-Soo Cho, Kyun-Do Kim, Byung-Ha Oh

Affiliations

  1. Department of Biological Sciences, Kaist Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
  2. Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
  3. Center for Convergent Research of Emerging Virus Infection, Korea Research Institute of Chemical Technology, Daejeon, Republic of Korea.
  4. Institute for Protein Innovation, Boston, MA, USA.
  5. Division of Hematology-Oncology, Boston Children's Hospital, Harvard Medical School, Boston, MA, USA.
  6. Molecular Engineering & Sciences Institute & Institute for Protein Design, University of Washington, Seattle, Washington, USA.

PMID: 35030983 DOI: 10.1080/19420862.2021.2021601

Abstract

Coronavirus disease 2019, caused by SARS-CoV-2, remains an on-going pandemic, partly due to the emergence of variant viruses that can "break-through" the protection of the current vaccines and neutralizing antibodies (nAbs), highlighting the needs for broadly nAbs and next-generation vaccines. We report an antibody that exhibits breadth and potency in binding the receptor-binding domain (RBD) of the virus spike glycoprotein across SARS coronaviruses. Initially, a lead antibody was computationally discovered and crystallographically validated that binds to a highly conserved surface of the RBD of wild-type SARS-CoV-2. Subsequently, through experimental affinity enhancement and computational affinity maturation, it was further developed to bind the RBD of all concerning SARS-CoV-2 variants, SARS-CoV-1 and pangolin coronavirus with pico-molar binding affinities, consistently exhibited strong neutralization activity against wild-type SARS-CoV-2 and the Alpha and Delta variants. These results identify a vulnerable target site on coronaviruses for development of pan-sarbecovirus nAbs and vaccines.

Keywords: Computational antibody discovery; Sars-CoV-2; broad-spectrum vaccine; broadly neutralizing antibody; emerging variants

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