ArticleThe Journal of biological chemistry2012
Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 53 citations in OpenAlex.
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- Site-specific glycosylation of SARS-CoV-2: Big challenges in mass spectrometry analysis.Proteomics · 2022Review
- Glycosylation of SARS-CoV-2: structural and functional insights.Analytical and bioanalytical chemistry · 2021Review
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Modulating the quantity of HIV Env-specific CD4 T cell help promotes rare B cell responses in germinal centers.The Journal of experimental medicine · 2021Article
- Visualization of the HIV-1 Env glycan shield across scales.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition.Scientific reports · 2020Article
- Analysis of the SARS-CoV-2 spike protein glycan shield: implications for immune recognition.bioRxiv : the preprint server for biology · 2020Article
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- Global site-specific N-glycosylation analysis of HIV envelope glycoprotein.Nature communications · 2017Article
- Minimally Mutated HIV-1 Broadly Neutralizing Antibodies to Guide Reductionist Vaccine Design.PLoS pathogens · 2016Article
- Influenza Virus Hemagglutinin Glycoproteins with Different N-Glycan Patterns Activate Dendritic Cells In Vitro.Journal of virology · 2016Article
- Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein.Cell reports · 2016Article
- Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion.Viruses · 2016Review
- Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy.Structure (London, England : 1993) · 2015Article
- Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.Nature communications · 2015Article
- A New Approach to Produce HIV-1 Envelope Trimers: BOTH CLEAVAGE AND PROPER GLYCOSYLATION ARE ESSENTIAL TO GENERATE AUTHENTIC TRIMERS.The Journal of biological chemistry · 2015Article
- HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers.Science (New York, N.Y.) · 2015Article
Corrections and comments
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Authors and funding
17 authors at 3 institutions in 2 countries.
Funding
Abstract
The trimeric envelope glycoprotein complex (Env) is the focus of vaccine development programs aimed at generating protective humoral responses to human immunodeficiency virus type 1 (HIV-1). N-Linked glycans, which constitute almost half of the molecular mass of the external Env domains, produce considerable structural heterogeneity and are a major impediment to crystallization studies. Moreover, by shielding the peptide backbone, glycans can block attempts to generate neutralizing antibodies against a substantial subset of potential epitopes when Env proteins are used as immunogens. Here, we describe the partial deglycosylation of soluble, cleaved recombinant Env trimers by inhibition of the synthesis of complex N-glycans during Env production, followed by treatment with glycosidases under conditions that preserve Env trimer integrity. The partially deglycosylated trimers are stable, and neither abnormally sensitive to proteolytic digestion nor prone to aggregation. Moreover, the deglycosylated trimers retain or increase their ability to bind CD4 and antibodies that are directed to conformational epitopes, including the CD4-binding site and the V3 region. However, as expected, they do not react with glycan-dependent antibodies 2G12 and PGT123, or the C-type lectin receptor DC-SIGN. Electron microscopic analysis shows that partially deglycosylated trimers have a structure similar to fully glycosylated trimers, indicating that removal of glycans does not substantially perturb the structural integrity of the trimer. The glycan-depleted Env trimers should be useful for structural and immunogenicity studies.
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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.