ArticleJournal of virology2019
Defining HIV-1 Envelope N-Glycan Microdomains through Site-Specific Heterogeneity Profiles.
Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- Identification of a potent V3 glycan site broadly neutralizing antibody targeting an N332Nature immunology · 2026Article
- Identity, functional consequences, and context effects of amino acids inserted during suppression of CFTR nonsense mutations.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2026Article
- Bridging Viral Glycobiology and Lectin Biotechnology for Antiviral and Diagnostic Strategies.ACS bio & med chem Au · 2025Review
- Identification of a broad and potent V3 glycan site bNAb targeting an N332bioRxiv : the preprint server for biology · 2025Article
- Beyond glycan barriers: non-cognate ligands and protein mimicry approaches to elicit broadly neutralizing antibodies for HIV-1.Journal of biomedical science · 2024Review
- HIV-1 interaction with aniScience · 2024Article
- Glycosylation of ALV-J Envelope Protein at Sites 17 and 193 Is Pivotal in the Virus Infection.Journal of virology · 2022Article
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Quantitative assessment of successive carbohydrate additions to the clustered O-glycosylation sites of IgA1 by glycosyltransferases.Glycobiology · 2021Article
- Mass Spectrometry-Based Structural Virology.Analytical chemistry · 2021Review
- Sequential Analysis of the N/O-Glycosylation of Heavily Glycosylated HIV-1 gp120 Using EThcD-sceHCD-MS/MS.Frontiers in immunology · 2021Article
- Quantification of the Resilience and Vulnerability of HIV-1 Native Glycan Shield at Atomistic Detail.iScience · 2020Article
- Glycan Positioning Impacts HIV-1 Env Glycan-Shield Density, Function, and Recognition by Antibodies.iScience · 2020Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Vulnerabilities in coronavirus glycan shields despite extensive glycosylation.Nature communications · 2020Article
- Mass spectrometry for the identification and analysis of highly complex glycosylation of therapeutic or pathogenic proteins.Expert review of proteomics · 2020Review
- Proteins mimicking epitope of HIV-1 virus neutralizing antibody induce virus-neutralizing sera in mice.EBioMedicine · 2019Article
- Glycosylation of viral surface proteins probed by mass spectrometry.Current opinion in virology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 1 institution in 2 countries.
Funding
Abstract
The HIV-1 envelope (Env) glycans shield the surface of Env from the immune system and form integral interactions important for a functional Env. To understand how individual N-glycosylation sites (NGS) coordinate to form a dynamic shield and evade the immune system through mutations, we tracked 20 NGS in Env from HIV-transmitted/founder (T/F) and immune escape variants and their mutants involving the N262 glycan. NGS were profiled in a site-specific manner using a high-resolution mass spectrometry (MS)-based workflow. Using this site-specific quantitative heterogeneity profiling, we empirically characterized the interdependent NGS of a microdomain in the high-mannose patch (HMP). The changes (shifts) in NGS heterogeneity between the T/F and immune escape variants defined a range of NGS that we further probed for exclusive combinations of sequons in the HMP microdomain using the Los Alamos National Laboratory HIV sequence database. The resultant sequon combinations, including the highly conserved NGS N262, N448, and N301, created an immune escape map of the conserved and variable sequons in the HMP microdomain. This report provides details on how some clustered NGS form microdomains that can be identified and tracked across Env variants. These microdomains have a limited number of N-glycan-sequon combinations that may allow the anticipation of immune escape variants.
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What OpenQuestion holds
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.