IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v584y2020i7819d10.1038_s41586-020-2380-z.html
   My bibliography  Save this article

Human neutralizing antibodies elicited by SARS-CoV-2 infection

Author

Listed:
  • Bin Ju

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
    Southern University of Science and Technology)

  • Qi Zhang

    (Tsinghua University)

  • Jiwan Ge

    (Tsinghua University)

  • Ruoke Wang

    (Tsinghua University)

  • Jing Sun

    (State Key Laboratory of Respiratory Disease, National Clinical Research Center for Respiratory Disease, Guangzhou Institute of Respiratory Health, the First Affiliated Hospital of Guangzhou Medical University)

  • Xiangyang Ge

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Jiazhen Yu

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Sisi Shan

    (Tsinghua University)

  • Bing Zhou

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Shuo Song

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Xian Tang

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Jinfang Yu

    (Tsinghua University)

  • Jun Lan

    (Tsinghua University)

  • Jing Yuan

    (Shenzhen Third People’s Hospital)

  • Haiyan Wang

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital)

  • Juanjuan Zhao

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
    Southern University of Science and Technology)

  • Shuye Zhang

    (Fudan University)

  • Youchun Wang

    (Division of HIV/AIDS and Sex-Transmitted Virus Vaccines, National Institutes for Food and Drug Control)

  • Xuanling Shi

    (Tsinghua University)

  • Lei Liu

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
    Southern University of Science and Technology)

  • Jincun Zhao

    (State Key Laboratory of Respiratory Disease, National Clinical Research Center for Respiratory Disease, Guangzhou Institute of Respiratory Health, the First Affiliated Hospital of Guangzhou Medical University)

  • Xinquan Wang

    (Tsinghua University)

  • Zheng Zhang

    (Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People’s Hospital
    Southern University of Science and Technology)

  • Linqi Zhang

    (Tsinghua University)

Abstract

The coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a global health emergency that is in urgent need of intervention1–3. The entry of SARS-CoV-2 into its target cells depends on binding between the receptor-binding domain (RBD) of the viral spike protein and its cellular receptor, angiotensin-converting enzyme 2 (ACE2)2,4–6. Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2. We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD. Unexpectedly, the anti-SARS-CoV-2 antibodies and the infected plasma did not cross-react with the RBDs of SARS-CoV or Middle East respiratory syndrome-related coronavirus (MERS-CoV), although there was substantial plasma cross-reactivity to their trimeric spike proteins. Analysis of the crystal structure of RBD-bound antibody revealed that steric hindrance inhibits viral engagement with ACE2, thereby blocking viral entry. These findings suggest that anti-RBD antibodies are largely viral-species-specific inhibitors. The antibodies identified here may be candidates for development of clinical interventions against SARS-CoV-2.

Suggested Citation

  • Bin Ju & Qi Zhang & Jiwan Ge & Ruoke Wang & Jing Sun & Xiangyang Ge & Jiazhen Yu & Sisi Shan & Bing Zhou & Shuo Song & Xian Tang & Jinfang Yu & Jun Lan & Jing Yuan & Haiyan Wang & Juanjuan Zhao & Shuy, 2020. "Human neutralizing antibodies elicited by SARS-CoV-2 infection," Nature, Nature, vol. 584(7819), pages 115-119, August.
    • Handle: RePEc:nat:nature:v:584:y:2020:i:7819:d:10.1038_s41586-020-2380-z
    DOI: 10.1038/s41586-020-2380-z
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-020-2380-z
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/s41586-020-2380-z?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Oscar Guzmán-Martínez & Kathia Guardado & Miguel Varela-Cardoso & Alejandro Trujillo-Rivera & Iván Gómez-Ñañez & María Cristina Ortiz-León & Rafaela Espinosa & Celso Ramos & Julio Isael Pérez-Carreón , 2021. "Potential Protection of Pre-Existent Antibodies to Human Coronavirus 229E on COVID-19 Severity," IJERPH, MDPI, vol. 18(17), pages 1-9, August.
    2. Bin Ju & Qing Fan & Miao Wang & Xuejiao Liao & Huimin Guo & Haiyan Wang & Xiangyang Ge & Lei Liu & Zheng Zhang, 2022. "Antigenic sin of wild-type SARS-CoV-2 vaccine shapes poor cross-neutralization of BA.4/5/2.75 subvariants in BA.2 breakthrough infections," Nature Communications, Nature, vol. 13(1), pages 1-6, December.
    3. Yifan Wang & Caixuan Liu & Chao Zhang & Yanxing Wang & Qin Hong & Shiqi Xu & Zuyang Li & Yong Yang & Zhong Huang & Yao Cong, 2022. "Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Mendoza, Daniel E. & Ochoa-Sánchez, Ana & Samaniego, Esteban P., 2022. "Forecasting of a complex phenomenon using stochastic data-based techniques under non-conventional schemes: The SARS-CoV-2 virus spread case," Chaos, Solitons & Fractals, Elsevier, vol. 158(C).
    5. Mingxi Li & Yifei Ren & Zhen Qin Aw & Bo Chen & Ziqing Yang & Yuqing Lei & Lin Cheng & Qingtai Liang & Junxian Hong & Yiling Yang & Jing Chen & Yi Hao Wong & Jing Wei & Sisi Shan & Senyan Zhang & Jiwa, 2022. "Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecoviruses," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    6. Yanqun Wang & An Yan & Deyong Song & Maoqin Duan & Chuangchuang Dong & Jiantao Chen & Zihe Jiang & Yuanzhu Gao & Muding Rao & Jianxia Feng & Zhaoyong Zhang & Ruxi Qi & Xiaomin Ma & Hong Liu & Beibei Y, 2024. "Identification of a highly conserved neutralizing epitope within the RBD region of diverse SARS-CoV-2 variants," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    7. Caitlin I. Stoddard & Kevin Sung & Zak A. Yaffe & Haidyn Weight & Guillaume Beaudoin-Bussières & Jared Galloway & Soren Gantt & Judith Adhiambo & Emily R. Begnel & Ednah Ojee & Jennifer Slyker & Dalto, 2023. "Elevated binding and functional antibody responses to SARS-CoV-2 in infants versus mothers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    8. Tomohiro Takano & Takashi Sato & Ryutaro Kotaki & Saya Moriyama & Shuetsu Fukushi & Masahiro Shinoda & Kiyomi Kabasawa & Nagashige Shimada & Mio Kousaka & Yu Adachi & Taishi Onodera & Kazutaka Terahar, 2023. "Heterologous SARS-CoV-2 spike protein booster elicits durable and broad antibody responses against the receptor-binding domain," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    9. Danique M. H. Rijswijck & Albert Bondt & Max Hoek & Karlijn Straten & Tom G. Caniels & Meliawati Poniman & Dirk Eggink & Chantal Reusken & Godelieve J. Bree & Rogier W. Sanders & Marit J. Gils & Alber, 2022. "Discriminating cross-reactivity in polyclonal IgG1 responses against SARS-CoV-2 variants of concern," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    10. Andrew C. Hunt & Bastian Vögeli & Ahmed O. Hassan & Laura Guerrero & Weston Kightlinger & Danielle J. Yoesep & Antje Krüger & Madison DeWinter & Michael S. Diamond & Ashty S. Karim & Michael C. Jewett, 2023. "A rapid cell-free expression and screening platform for antibody discovery," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:584:y:2020:i:7819:d:10.1038_s41586-020-2380-z. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.