ArticleVirology2008
Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity.
Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 54 citations in OpenAlex.
- Structural determination of the HIV-1 Variable Region 3 epitope of antibody 19b.Journal of virology · 2026Article
- Membrane HIV-1 envelope glycoproteins stabilized more strongly in a pretriggered conformation than natural virus Envs.iScience · 2024Article
- Anti-HIV-1 Nanobody-IgG1 Constructs With Improved Neutralization Potency and the Ability to Mediate Fc Effector Functions.Frontiers in immunology · 2022Article
- Isolation of Neutralizing Human Single Chain Antibodies Against Conserved Hemagglutinin Epitopes of Influenza a Virus H3N2 Strain.Reports of biochemistry & molecular biology · 2019Article
- Article
- Analysis of HIV-1 envelope evolution suggests antibody-mediated selection of common epitopes among Chinese former plasma donors from a narrow-source outbreak.Scientific reports · 2018Article
- Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers.The Journal of biological chemistry · 2018Article
- Prediction of HIV-associated neurocognitive disorder (HAND) from three genetic features of envelope gp120 glycoprotein.Retrovirology · 2018Article
- Display of the HIV envelope protein at the yeast cell surface for immunogen development.PloS one · 2018Article
- Functional Stability of HIV-1 Envelope Trimer Affects Accessibility to Broadly Neutralizing Antibodies at Its Apex.Journal of virology · 2017Article
- Accurate predictions of population-level changes in sequence and structural properties of HIV-1 Env using a volatility-controlled diffusion model.PLoS biology · 2017Article
- Ibalizumab Targeting CD4 Receptors, An Emerging Molecule in HIV Therapy.Frontiers in microbiology · 2017Review
- Antigenic variability: Obstacles on the road to vaccines against traditionally difficult targets.Human vaccines & immunotherapeutics · 2016Review
- Current Advances in Virus-Like Particles as a Vaccination Approach against HIV Infection.Vaccines · 2016Review
- Polyreactivity and autoreactivity among HIV-1 antibodies.Journal of virology · 2015Article
- Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- CD4-mimetic small molecules sensitize human immunodeficiency virus to vaccine-elicited antibodies.Journal of virology · 2014Article
- Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120.Journal of virology · 2013Article
- Characterization of humoral responses to soluble trimeric HIV gp140 from a clade A Ugandan field isolate.Journal of translational medicine · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The V3 loop of HIV-1 gp120 is considered occluded on many primary viruses. However, virus sensitivity to neutralization by different V3 mAbs often varies, indicating that access to V3 is not restricted equally for all antibodies. Here, we have sought to gain a better understanding of these restrictions by determining the neutralizing activities of 7 V3 mAbs (19b, 39F, CO11, F2A3, F530, LA21, and LE311) against 15 subtype B primary isolates and relating these activities to the fine specificity of the mAbs. Not surprisingly, we found that most mAbs neutralized the same 2-3 viruses, with only mAb F530 able to neutralize 2 additional viruses not neutralized by the other mAbs. Epitope mapping revealed that positively-charged residues in or near the V3 stem are important for the binding of all the mAbs and that most mAbs seem to require the Pro residue that forms the GPGR beta hairpin turn in the V3 tip for binding. Based on the mapping, we determined that V3 sequence variation accounted for neutralization resistance of approximately half the viruses tested. Comparison of these results to those of select V3 mAbs with overall better neutralizing activities in the light of structural information illustrates how an antibody's mode of interaction with V3, driven by contact residue requirements, may restrict the antibody from accessing its epitope on different viruses. Based on the data we propose an angle of interaction with V3 that is less stringent on access for antibodies with cross-neutralizing activity compared to antibodies that neutralize relatively fewer viruses.
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