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Networks of HIV-1 Envelope Glycans Maintain Antibody Epitopes in the Face of Glycan Additions and Deletions

  1. Author:
    Seabright, Gemma E
    Cottrell, Christopher A
    van Gils, Marit J
    D'addabbo, Alessio
    Harvey, David J
    Behrens, Anna-Janina
    Allen, Joel D
    Watanabe, Yasunori
    Scaringi, Nicole
    Polveroni, Thomas M
    Maker, Allison
    Vasiljevic, Snezana
    De Val Alda,Natalia
    Sanders, Rogier W
    Ward, Andrew B
    Crispin, Max

  2. Author Address

    School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK., Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA 92037, USA., Department of Medical Microbiology, Amsterdam UMC, AMC, University of Amsterdam, Amsterdam 1105 AZ, The Netherlands., School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK., School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK; Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Old Road Campus, Oxford OX3 7FZ, UK., Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Leidos Biomedical Research Inc., Frederick, MD 21701, USA; Center for Molecular Microscopy, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA., Department of Medical Microbiology, Amsterdam UMC, AMC, University of Amsterdam, Amsterdam 1105 AZ, The Netherlands; Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA., School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. Electronic address: max.crispin@soton.ac.uk.,
    1. Year: 2020
    2. Date: AUG 4
    3. Epub Date: 2020 05 12
  2. Journal: Structure (London, England : 1993)
    1. 28
    2. 8
    3. Pages: 897-+
  4. Type of Article: Article
  5. ISSN: 0969-2126
  1. Abstract:

    Numerous broadly neutralizing antibodies (bnAbs) have been identified that target the glycans of the HIV-1 envelope spike. Neutralization breadth is notable given that glycan processing can be substantially influenced by the presence or absence of neighboring glycans. Here, using a stabilized recombinant envelope trimer, we investigate the degree to which mutations in the glycan network surrounding an epitope impact the fine glycan processing of antibody targets. Using cryo-electron microscopy and site-specific glycan analysis, we reveal the importance of glycans in the formation of the 2G12 bnAb epitope and show that the epitope is only subtly impacted by variations in the glycan network. In contrast, we show that the PG9 and PG16 glycan-based epitopes at the trimer apex are dependent on the presence of the highly conserved surrounding glycans. Glycan networks underpin the conservation of bnAb epitopes and are an important parameter in immunogen design. Copyright © 2020 The Author(s). Published by Elsevier Ltd.. All rights reserved.

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.str.2020.04.022
  3. PMID: 32433992
  4. View record in Web of Science®
  5. WOS: 000557639900005
  6. PII : S0969-2126(20)30168-4

Library Notes

  1. Fiscal Year: FY2019-2020
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