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Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses

Author

Listed:
  • Gabriela Alvarado

    (Vanderbilt University Medical Center)

  • Wilhelm Salmen

    (Baylor College of Medicine)

  • Khalil Ettayebi

    (Baylor College of Medicine)

  • Liya Hu

    (The Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine)

  • Banumathi Sankaran

    (Berkeley Center for Structural Biology, Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley Laboratory)

  • Mary K. Estes

    (Baylor College of Medicine
    Baylor College of Medicine)

  • B. V. Venkataram Prasad

    (Baylor College of Medicine
    The Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine)

  • James E. Crowe

    (Vanderbilt University Medical Center
    The Vanderbilt Vaccine Center, Vanderbilt University Medical Center
    Vanderbilt University Medical Center)

Abstract

The rational development of norovirus vaccine candidates requires a deep understanding of the antigenic diversity and mechanisms of neutralization of the virus. Here, we isolate and characterize a panel of broadly cross-reactive naturally occurring human monoclonal IgMs, IgAs and IgGs reactive with human norovirus (HuNoV) genogroup I or II (GI or GII). We note three binding patterns and identify monoclonal antibodies (mAbs) that neutralize at least one GI or GII HuNoV strain when using a histo-blood group antigen (HBGA) blocking assay. The HBGA blocking assay and a virus neutralization assay using human intestinal enteroids reveal that the GII-specific mAb NORO-320, mediates HBGA blocking and neutralization of multiple GII genotypes. The Fab form of NORO-320 neutralizes GII.4 infection more potently than the mAb, however, does not block HBGA binding. The crystal structure of NORO-320 Fab in complex with GII.4 P-domain shows that the antibody recognizes a highly conserved region in the P-domain distant from the HBGA binding site. Dynamic light scattering analysis of GII.4 virus-like particles with mAb NORO-320 shows severe aggregation, suggesting neutralization is by steric hindrance caused by multivalent cross-linking. Aggregation was not observed with the Fab form of NORO-320, suggesting that this clone also has additional inhibitory features.

Suggested Citation

  • Gabriela Alvarado & Wilhelm Salmen & Khalil Ettayebi & Liya Hu & Banumathi Sankaran & Mary K. Estes & B. V. Venkataram Prasad & James E. Crowe, 2021. "Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24649-w
    DOI: 10.1038/s41467-021-24649-w
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    References listed on IDEAS

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    1. Sarah M Bartsch & Benjamin A Lopman & Sachiko Ozawa & Aron J Hall & Bruce Y Lee, 2016. "Global Economic Burden of Norovirus Gastroenteritis," PLOS ONE, Public Library of Science, vol. 11(4), pages 1-16, April.
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    Cited by:

    1. Liya Hu & Wilhelm Salmen & Rong Chen & Yi Zhou & Frederick Neill & James E. Crowe & Robert L. Atmar & Mary K. Estes & B. V. Venkataram Prasad, 2022. "Atomic structure of the predominant GII.4 human norovirus capsid reveals novel stability and plasticity," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. B. Vijayalakshmi Ayyar & Khalil Ettayebi & Wilhelm Salmen & Umesh C. Karandikar & Frederick H. Neill & Victoria R. Tenge & Sue E. Crawford & Erhard Bieberich & B. V. Venkataram Prasad & Robert L. Atma, 2023. "CLIC and membrane wound repair pathways enable pandemic norovirus entry and infection," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Wilhelm Salmen & Liya Hu & Marina Bok & Natthawan Chaimongkol & Khalil Ettayebi & Stanislav V. Sosnovtsev & Kaundal Soni & B. Vijayalakshmi Ayyar & Sreejesh Shanker & Frederick H. Neill & Banumathi Sa, 2023. "A single nanobody neutralizes multiple epochally evolving human noroviruses by modulating capsid plasticity," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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