ArticlePloS one2013
The influence of N-linked glycans on the molecular dynamics of the HIV-1 gp120 V3 loop.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Prediction of the Co-receptor usage of the main worldwide HIV-1 subtypes, CRF, and CRF35-AD in Iranian patients via the five genotypic tools.Biochemistry and biophysics reports · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Integration of Experimental and Computational Methods to Characterize Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Structure-Based Identification of Natural-Product-Derived Compounds with Potential to Inhibit HIV-1 Entry.Molecules (Basel, Switzerland) · 2023Article
- Glycosylation and the global virome.Molecular ecology · 2023Article
- HIV-1 Envelope Conformation, Allostery, and Dynamics.Viruses · 2021Review
- Visualization of the HIV-1 Env glycan shield across scales.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Leveraging glycomics data in glycoprotein 3D structure validation with Privateer.Beilstein journal of organic chemistry · 2020Article
- Impact of branching on the conformational heterogeneity of the lipopolysaccharide from Klebsiella pneumoniae: Implications for vaccine design.Carbohydrate research · 2019Article
- Predicting the Structures of Glycans, Glycoproteins, and Their Complexes.Chemical reviews · 2018Review
- All-atom virus simulations.Current opinion in virology · 2018Review
- Computational study of HIV gp120 as a target for polyanionic entry inhibitors: Exploiting the V3 loop region.PloS one · 2018Article
- Conformational Heterogeneity of the HIV Envelope Glycan Shield.Scientific reports · 2017Article
- Partial HIV C2V3 envelope sequence analysis reveals association of coreceptor tropism, envelope glycosylation and viral genotypic variability among Kenyan patients on HAART.Virology journal · 2017Article
- Protein structural disorder of the envelope V3 loop contributes to the switch in human immunodeficiency virus type 1 cell tropism.PloS one · 2017Article
- Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.PLoS computational biology · 2016Article
- Roles of glycans in interactions between gp120 and HIV broadly neutralizing antibodies.Glycobiology · 2016Article
- Characterizing the Diverse Mutational Pathways Associated with R5-Tropic Maraviroc Resistance: HIV-1 That Uses the Drug-Bound CCR5 Coreceptor.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
N-linked glycans attached to specific amino acids of the gp120 envelope trimer of a HIV virion can modulate the binding affinity of gp120 to CD4, influence coreceptor tropism, and play an important role in neutralising antibody responses. Because of the challenges associated with crystallising fully glycosylated proteins, most structural investigations have focused on describing the features of a non-glycosylated HIV-1 gp120 protein. Here, we use a computational approach to determine the influence of N-linked glycans on the dynamics of the HIV-1 gp120 protein and, in particular, the V3 loop. We compare the conformational dynamics of a non-glycosylated gp120 structure to that of two glycosylated gp120 structures, one with a single, and a second with five, covalently linked high-mannose glycans. Our findings provide a clear illustration of the significant effect that N-linked glycosylation has on the temporal and spatial properties of the underlying protein structure. We find that glycans surrounding the V3 loop modulate its dynamics, conferring to the loop a marked propensity towards a more narrow conformation relative to its non-glycosylated counterpart. The conformational effect on the V3 loop provides further support for the suggestion that N-linked glycosylation plays a role in determining HIV-1 coreceptor tropism.
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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.