ArticleProceedings of the National Academy of Sciences of the United States of America2010
Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers.
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Who cites it
230 citing papers in PubMed, 339 citations in OpenAlex.
- Structural Insights Into ManAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Decoding the glycan shield: Immune recognition and response to the HIV-1 envelope trimer.The Journal of biological chemistry · 2026Review
- Differential contributions of human oligosaccharyltransferase complexes OST-A and OST-B to HIV-1 envelope glycoprotein glycosylation.Journal of virology · 2026Article
- Comparing CD8+ T cell ENV epitopes of two HLA class I alleles associated with different outcomes of HIV-1 infection with broadly neutralizing antibodies epitope targets discovered to date.Frontiers in immunology · 2026Article
- Carbohydrate-Binding Mechanism and Therapeutic Potential of Lectin Mimics.Advances in experimental medicine and biology · 2026Review
- Germline-Targeting Strategies to Induce bNAbs against HIV-1.Current HIV research · 2026Review
- Framework-mediated binding of foreign and self-glycans by IGHV4-34 antibodies.Frontiers in immunology · 2026Review
- Glycan-reactive antibodies isolated from human HIV-1 vaccine trial participants show broad pathogen cross-reactivity.Journal of virology · 2025Article
- Bridging Viral Glycobiology and Lectin Biotechnology for Antiviral and Diagnostic Strategies.ACS bio & med chem Au · 2025Review
- Factors associated with resistance of HIV-1 reservoir viruses to neutralization by autologous IgG antibodies.The Journal of clinical investigation · 2025Article
- Article
- A B cell screen against endogenous retroviruses identifies glycan-reactive IgM that recognizes a broad array of enveloped viruses.Science immunology · 2024Article
- Isolation and characterization of IgG3 glycan-targeting antibodies with exceptional cross-reactivity for diverse viral families.PLoS pathogens · 2024Article
- HIV-1 interaction with aniScience · 2024Article
- Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024Review
- Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate.Nature communications · 2024Article
- Impact of stabilizing mutations on the antigenic profile and glycosylation of membrane-expressed HIV-1 envelope glycoprotein.PLoS pathogens · 2023Article
- Conformations of Human Immunodeficiency Virus Envelope Glycoproteins in Detergents and Styrene-Maleic Acid Lipid Particles.Journal of virology · 2023Article
- Review
- Optimizing the Production of gp145, an HIV-1 Envelope Glycoprotein Vaccine Candidate and Its Encapsulation in Guanosine Microparticles.Vaccines · 2023Article
170 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The envelope spike of HIV is one of the most highly N-glycosylated structures found in nature. However, despite extensive research revealing essential functional roles in infection and immune evasion, the chemical structures of the glycans on the native viral envelope glycoprotein gp120--as opposed to recombinantly generated gp120--have not been described. Here, we report on the identity of the N-linked glycans from primary isolates of HIV-1 (clades A, B, and C) and from the simian immunodeficiency virus. MS analysis reveals a remarkably simple and highly conserved virus-specific glycan profile almost entirely devoid of medial Golgi-mediated processing. In stark contrast to recombinant gp120, which shows extensive exposure to cellular glycosylation enzymes (>70% complex type glycans), the native envelope shows barely detectable processing beyond the biosynthetic intermediate Man5GlcNAc2 (<2% complex type glycans). This oligomannose (Man5-9GlcNAc2) profile is conserved across primary isolates and geographically divergent clades but is not reflected in the current generation of gp120 antigens used for vaccine trials. In the context of vaccine design, we also note that Manalpha1-->2Man-terminating glycans (Man6-9GlcNAc2) of the type recognized by the broadly neutralizing anti-HIV antibody 2G12 are 3-fold more abundant on the native envelope than on the recombinant monomer and are also found on isolates not neutralized by 2G12. The Manalpha1-->2Man residues of gp120 therefore provide a vaccine target that is physically larger and antigenically more conserved than the 2G12 epitope itself. This study revises and extends our understanding of the glycan shield of HIV with implications for AIDS vaccine design.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.