ArticleScientific reports2018
Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a Glycan.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Geographic Influence on Secondary Metabolite Profiles in Leaves of the EndemicInternational journal of molecular sciences · 2026Article
- Decoding the glycan shield: Immune recognition and response to the HIV-1 envelope trimer.The Journal of biological chemistry · 2026Review
- Glycoprofile Comparison of the SARS-CoV-2 Spike Proteins Expressed in CHO and HEK Cell Lines.Molecular biotechnology · 2025Article
- Structure and antigenicity of divergent Henipavirus fusion glycoproteins.Nature communications · 2023Article
- Glycosylation and the global virome.Molecular ecology · 2023Article
- Characterization and immunogenicity of SARS-CoV-2 spike proteins with varied glycosylation.Vaccine · 2022Article
- Stabilized HIV-1 envelope immunization induces neutralizing antibodies to the CD4bs and protects macaques against mucosal infection.Science translational medicine · 2022Article
- Development of Martini 2.2 parameters for N-glycans: a case study of the HIV-1 Env glycoprotein dynamics.Glycobiology · 2021Article
- HIV-1 Envelope Conformation, Allostery, and Dynamics.Viruses · 2021Review
- Glycans in Virus-Host Interactions: A Structural Perspective.Frontiers in molecular biosciences · 2021Review
- Quantification of the Resilience and Vulnerability of HIV-1 Native Glycan Shield at Atomistic Detail.iScience · 2020Article
- Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies.iScience · 2020Article
- Visualization of the HIV-1 Env glycan shield across scales.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor.Cell host & microbe · 2020Article
- Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor.bioRxiv : the preprint server for biology · 2020Article
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Authors and funding
7 authors.
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Abstract
The HIV-1 envelope (Env) glycoprotein is the primary target of the humoral immune response and a critical vaccine candidate. However, Env is densely glycosylated and thereby substantially protected from neutralisation. Importantly, glycan N301 shields V3 loop and CD4 binding site epitopes from neutralising antibodies. Here, we use molecular dynamics techniques to evaluate the structural rearrangements that maintain the protective qualities of the glycan shield after the loss of glycan N301. We examined a naturally occurring subtype C isolate and its N301A mutant; the mutant not only remained protected against neutralising antibodies targeting underlying epitopes, but also exhibited an increased resistance to the VRC01 class of broadly neutralising antibodies. Analysis of this mutant revealed several glycans that were responsible, independently or through synergy, for the neutralisation resistance of the mutant. These data provide detailed insight into the glycan shield's ability to compensate for the loss of a glycan, as well as the cascade of glycan movements on a protomer, starting at the point mutation, that affects the integrity of an antibody epitope located at the edge of the diminishing effect. These results present key, previously overlooked, considerations for HIV-1 Env glycan research and related vaccine studies.
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