ArticleJournal of immunology (Baltimore, Md. : 1950)2009
Proximal glycans outside of the epitopes regulate the presentation of HIV-1 envelope gp120 helper epitopes.
Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Who cites it
34 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular mechanisms of immune evasion by host protein glycosylation of a bacterial immunogen used in nucleic acid vaccines.The Journal of biological chemistry · 2026Article
- Investigation of carbohydrate-based molecules ofFrontiers in veterinary science · 2026Article
- The Biological Role of Enveloped Virus Glycosylation and Its Interactions with Antiviral Lectins.Advances in experimental medicine and biology · 2026Review
- Antigen presentation of post-translationally modified peptides in major histocompatibility complexes.Immunology and cell biology · 2025Review
- Protein Glycosylation Patterns Shaped By the IRE1-XBP1s Arm of the Unfolded Protein Response.Israel journal of chemistry · 2024Article
- Structural Framework for Analysis of CD4+ T-Cell Epitope Dominance in Viral Fusion Proteins.Biochemistry · 2023Review
- Influence of N-glycosylation in the A and C domains on the immunogenicity of factor VIII.Blood advances · 2022Article
- Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants.PLoS pathogens · 2022Review
- Chemoenzymatic Synthesis of Complex N-Glycans of the Parasite S. mansoni to Examine the Importance of Epitope Presentation on DC-SIGN recognition.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- Glycopeptide epitope facilitates HIV-1 envelope specific humoral immune responses by eliciting T cell help.Nature communications · 2020Article
- Env Exceptionalism: Why Are HIV-1 Env Glycoproteins Atypical Immunogens?Cell host & microbe · 2020Review
- Neutralizing Antibody Induction by HIV-1 Envelope Glycoprotein SOSIP Trimers on Iron Oxide Nanoparticles May Be Impaired by Mannose Binding Lectin.Journal of virology · 2020Article
- Why Glycosylation Matters in Building a Better Flu Vaccine.Molecular & cellular proteomics : MCP · 2019Review
- Article
- Metabolic labeling of HIV-1 envelope glycoprotein gp120 to elucidate the effect of gp120 glycosylation on antigen uptake.The Journal of biological chemistry · 2018Article
- Avian and Human Seasonal Influenza Hemagglutinin Proteins Elicit CD4 T Cell Responses That Are Comparable in Epitope Abundance and Diversity.Clinical and vaccine immunology : CVI · 2017Article
- Computer aided epitope design as a peptide vaccine component against Lassa virus.Bioinformation · 2017Article
- Structure/Function Studies Involving the V3 Region of the HIV-1 Envelope Delineate Multiple Factors That Affect Neutralization Sensitivity.Journal of virology · 2016Article
- Discrete partitioning of HIV-1 Env forms revealed by viral capture.Retrovirology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Glycosylation of HIV-1 envelope gp120 determines not only the proper structure, but also the immune responses against this Ag. Although glycans may be part of specific epitopes or shield other epitopes from T cells and Abs, this study provides evidence for a different immunomodulatory function of glycans associated with gp120 residues N230 and N448. These glycans are required for efficient MHC class II-restricted presentation of nearby CD4 T cell epitopes, even though they are not part of the epitopes. The glycans do not affect CD4 T cell recognition of more distant epitopes and are not essential for the proper folding and function of gp120. Data on CD4 T cell recognition of N448 mutants combined with proteolysis analyses and surface electrostatic potential calculation around residue N448 support the notion that N448 glycan near the epitope's C terminus renders the site to be surface accessible and allows its efficient processing. In contrast, the N230 glycan contributes to the nearby epitope presentation at a step other than the proteolytic processing of the epitope. Hence, N-glycans can determine CD4 T cell recognition of nearby gp120 epitopes by regulating the different steps in the MHC class II processing and presentation pathway after APCs acquire the intact gp120 Ag exogenously. Modifications of amino acids bearing glycans at the C termini of gp120 helper epitopes may prove to be a useful strategy for enhancing the immunogenicity of HIV-1 envelope gp120.
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Registered trials
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.