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Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies

  1. Author:
    Wei, Qing
    Hargett, Audra A
    Knoppova, Barbora
    Duverger, Alexandra
    Rawi, Reda
    Shen, Chen-Hsiang
    Farney, S Katie
    Hall, Stacy
    Brown, Rhubell
    Keele,Brandon
    Heath, Sonya L
    Saag, Michael S
    Kutsch, Olaf
    Chuang, Gwo-Yu
    Kwong, Peter D
    Moldoveanu, Zina
    Raska, Milan
    Renfrow, Matthew B
    Novak, Jan

  2. Author Address

    Department of Microbiology, University of Alabama at Birmingham, 845 19th Street S, Birmingham, AL 35294, USA., Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL, USA., Department of Medicine, University of Alabama at Birmingham, Birmingham, AL, USA., Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA., AIDS and Cancer Virus Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA., Department of Immunology, Palacky University Olomouc, Olomouc, Czech Republic.,
    1. Year: 2020
    2. Date: Nov 20
    3. Epub Date: 2020 10 21
  2. Journal: iScience
    1. 23
    2. 11
    3. Pages: 101711
  4. Type of Article: Article
  5. Article Number: 101711
  6. ISSN: 2589-0042
  1. Abstract:

    HIV-1 envelope (Env) N-glycosylation impact virus-cell entry and immune evasion. How each glycan interacts to shape the Env-protein-sugar complex and affects Env function is not well understood. Here, analysis of two Env variants from the same donor, with differing functional characteristics and N-glycosylation-site composition, revealed that changes to key N-glycosylation sites affected the Env structure at distant locations and had a ripple effect on Env-wide glycan processing, virus infectivity, antibody recognition, and virus neutralization. Specifically, the N262 glycan, although not in the CD4-binding site, modulated Env binding to the CD4 receptor, affected Env recognition by several glycan-dependent neutralizing antibodies, and altered site-specific glycosylation heterogeneity, with, for example, N448 displaying limited glycan processing. Molecular-dynamic simulations visualized differences in glycan density and how specific oligosaccharide positions can move to compensate for a glycan loss. This study demonstrates how changes in individual glycans can alter molecular dynamics, processing, and function of the Env-glycan shield. © 2020 The Author(s).

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External Sources

  1. View Full Text
  2. DOI: 10.1016/j.isci.2020.101711
  3. PMID: 33205023
  4. PMCID: PMC7649354
  5. View record in Web of Science®
  6. WOS: 000596692100003
  7. PII : S2589-0042(20)30908-1

Library Notes

  1. Fiscal Year: FY2020-2021
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