Selected article for: "heavy chain and monoclonal antibody"
Author: Banach, Bailey B.; Cerutti, Gabriele; Fahad, Ahmed S.; Shen, Chen-Hsiang; Oliveira De Souza, Matheus; Katsamba, Phinikoula S.; Tsybovsky, Yaroslav; Wang, Pengfei; Nair, Manoj S.; Huang, Yaoxing; Francino-Urdániz, Irene M.; Steiner, Paul J.; Gutiérrez-González, Matías; Liu, Lihong; López Acevedo, Sheila N.; Nazzari, Alexandra F.; Wolfe, Jacy R.; Luo, Yang; Olia, Adam S.; Teng, I-Ting; Yu, Jian; Zhou, Tongqing; Reddem, Eswar R.; Bimela, Jude; Pan, Xiaoli; Madan, Bharat; Laflin, Amy D.; Nimrania, Rajani; Yuen, Kwok-Yung; Whitehead, Timothy A.; Ho, David D.; Kwong, Peter D.; Shapiro, Lawrence; DeKosky, Brandon J.
Title: Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses
  • Cord-id: zv29vo8c
  • Document date: 2021_9_28
    • ID: zv29vo8c
    Snippet: Understanding mechanisms of protective antibody recognition can inform vaccine and therapeutic strategies against SARS-CoV-2. We report a monoclonal antibody, 910-30, targeting the SARS-CoV-2 receptor-binding site for ACE2 as a member of a public antibody response encoded by IGHV3-53/IGHV3-66 genes. Sequence and structural analyses of 910-30 and related antibodies explore how class recognition features correlate with SARS-CoV-2 neutralization. Cryo-EM structures of 910-30 bound to the SARS-CoV-2
    Document: Understanding mechanisms of protective antibody recognition can inform vaccine and therapeutic strategies against SARS-CoV-2. We report a monoclonal antibody, 910-30, targeting the SARS-CoV-2 receptor-binding site for ACE2 as a member of a public antibody response encoded by IGHV3-53/IGHV3-66 genes. Sequence and structural analyses of 910-30 and related antibodies explore how class recognition features correlate with SARS-CoV-2 neutralization. Cryo-EM structures of 910-30 bound to the SARS-CoV-2 spike trimer reveal binding interactions and its ability to disassemble spike. Despite heavy-chain sequence similarity, biophysical analyses of IGHV3-53/3-66-encoded antibodies highlight the importance of native heavy:light pairings for ACE2-binding competition and SARS-CoV-2 neutralization. We develop paired heavy:light class sequence signatures and determine antibody precursor prevalence to be ∼1 in 44,000 human B cells, consistent with public antibody identification in several convalescent COVID-19 patients. These class signatures reveal genetic, structural, and functional immune features that are helpful in accelerating antibody-based medical interventions for SARS-CoV-2.

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