ArticleCell reports2015
Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers.
Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed.
- HIV-1 Env Heterogeneity: Cleavage, Trafficking, and Antigenic Consequences for Virions and Infected Cells.Viruses · 2026Review
- Endocytic motif on HIV-1 Env regulates cleavage status and antibody neutralization of cell-free and cell-to-cell infection.Journal of virology · 2026Article
- Differential contributions of human oligosaccharyltransferase complexes OST-A and OST-B to HIV-1 envelope glycoprotein glycosylation.Journal of virology · 2026Article
- Spike conformational and glycan heterogeneity associated with furin cleavage causes incomplete neutralization of SARS-CoV-2.Nature communications · 2025Article
- The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.Nature reviews. Microbiology · 2025Review
- A B cell screen against endogenous retroviruses identifies glycan-reactive IgM that recognizes a broad array of enveloped viruses.Science immunology · 2024Article
- Generating and characterizing a comprehensive panel of CHO cells glycosylation mutants for advancing glycobiology and biotechnology research.Scientific reports · 2024Article
- Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity.PLoS pathogens · 2024Article
- Triple tandem trimer immunogens for HIV-1 and influenza nucleic acid-based vaccines.NPJ vaccines · 2024Article
- Signal peptide exchange alters HIV-1 envelope antigenicity and immunogenicity.Frontiers in immunology · 2024Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- Antigen pressure from two founder viruses induces multiple insertions at a single antibody position to generate broadly neutralizing HIV antibodies.PLoS pathogens · 2023Article
- Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.Retrovirology · 2023Article
- A plant-produced SARS-CoV-2 spike protein elicits heterologous immunity in hamsters.Frontiers in plant science · 2023Article
- Augmenting glycosylation-directed folding pathways enhances the fidelity of HIV Env immunogen production in plants.Biotechnology and bioengineering · 2022Article
- The diversity of the glycan shield of sarbecoviruses closely related to SARS-CoV-2.bioRxiv : the preprint server for biology · 2022Article
- A neutralizing antibody target in early HIV-1 infection was recapitulated in rhesus macaques immunized with the transmitted/founder envelope sequence.PLoS pathogens · 2022Article
- Review
- Epitope convergence of broadly HIV-1 neutralizing IgA and IgG antibody lineages in a viremic controller.The Journal of experimental medicine · 2022Article
- High thermostability improves neutralizing antibody responses induced by native-like HIV-1 envelope trimers.NPJ vaccines · 2022Article
46 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
A highly glycosylated, trimeric envelope glycoprotein (Env) mediates HIV-1 cell entry. The high density and heterogeneity of the glycans shield Env from recognition by the immune system, but paradoxically, many potent broadly neutralizing antibodies (bNAbs) recognize epitopes involving this glycan shield. To better understand Env glycosylation and its role in bNAb recognition, we characterized a soluble, cleaved recombinant trimer (BG505 SOSIP.664) that is a close structural and antigenic mimic of native Env. Large, unprocessed oligomannose-type structures (Man8-9GlcNAc2) are notably prevalent on the gp120 components of the trimer, irrespective of the mammalian cell expression system or the bNAb used for affinity purification. In contrast, gp41 subunits carry more highly processed glycans. The glycans on uncleaved, non-native oligomeric gp140 proteins are also highly processed. A homogeneous, oligomannose-dominated glycan profile is therefore a hallmark of a native Env conformation and a potential Achilles' heel that can be exploited for bNAb recognition and vaccine design.
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