ArticleThe Journal of biological chemistry2010
Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
What it found
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Who cites it
102 citing papers in PubMed, 148 citations in OpenAlex.
- Dual role of glycosylation in resistance to CD4-binding site broadly neutralizing antibodies.Journal of virology · 2026Article
- Comprehensive analysis of gp120 glycosylation to explore differences between transmitter/founder and chronic HIV-1 isolates.Glycobiology · 2026Article
- EZ-DMS - A Simple and Accessible Protocol and Software Package for Deep Mutational Scanning of Virus Proteins.bioRxiv : the preprint server for biology · 2026Article
- DC-SIGN (CD209)-mediated interactions between bacteria, lung cancer tissues, and macrophages promote cancer metastasis.Infectious agents and cancer · 2025Article
- Isolation and characterization of IgG3 glycan-targeting antibodies with exceptional cross-reactivity for diverse viral families.PLoS pathogens · 2024Article
- Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity.PLoS pathogens · 2024Article
- A VRC13-like bNAb response is associated with complex escape pathways in HIV-1 envelope.Journal of virology · 2024Article
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- DeGlyPHER: Highly sensitive site-specific analysis of N-linked glycans on proteins.Methods in enzymology · 2023Article
- Chemical tools to track and perturb the expression of sialic acid and fucose monosaccharides.Chemical communications (Cambridge, England) · 2022Review
- Sialic Acid and Fucose Residues on the SARS-CoV-2 Receptor-Binding Domain Modulate IgG Antibody Reactivity.ACS infectious diseases · 2022Article
- Glycan shield of the ebolavirus envelope glycoprotein GP.Communications biology · 2022Article
- Differential N- and O-glycosylation signatures of HIV-1 Gag virus-like particles and coproduced extracellular vesicles.Biotechnology and bioengineering · 2022Article
- Limited Variation between SARS-CoV-2-Infected Individuals in Domain Specificity and Relative Potency of the Antibody Response against the Spike Glycoprotein.Microbiology spectrum · 2022Article
- Myomedin replicas of gp120 V3 loop glycan epitopes recognized by PGT121 and PGT126 antibodies as non-cognate antigens for stimulation of HIV-1 broadly neutralizing antibodies.Frontiers in immunology · 2022Article
- Article
- Stable, high yield expression of gp145 Env glycoprotein from HIV-1 in mammalian cells.Biologicals : journal of the International Association of Biological Standardization · 2021Article
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Fejerlectin, a Lectin-like Peptide from the Skin ofACS omega · 2021Article
- HIV-1 Envelope Glycosylation and the Signal Peptide.Vaccines · 2021Review
42 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors at 5 institutions in 2 countries.
Funding
Abstract
Human immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design.
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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.