ArticleJournal of virology2011
The V1V2 domain and an N-linked glycosylation site in the V3 loop of the HIV-1 envelope glycoprotein modulate neutralization sensitivity to the human broadly neutralizing antibody 2G12.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Germline-somatic residue synergy reshapes antibody encounter-state pathways to enhance HIV-1 recognition.bioRxiv : the preprint server for biology · 2026Article
- A VRC13-like bNAb response is associated with complex escape pathways in HIV-1 envelope.Journal of virology · 2024Article
- Glycan dependent phenotype differences of HIV-1 generated from macrophage versus CD4Frontiers in immunology · 2023Article
- Signatures of immune selection in intact and defective proviruses distinguish HIV-1 elite controllers.Science translational medicine · 2021Article
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- Conformational Epitope-Specific Broadly Neutralizing Plasma Antibodies Obtained from an HIV-1 Clade C-Infected Elite Neutralizer Mediate Autologous Virus Escape through Mutations in the V1 Loop.Journal of virology · 2016Article
- Recent advances on the use of structural biology for the design of novel envelope immunogens of HIV-1.Current HIV research · 2013Article
- Molecular evolution of the HIV-1 Thai epidemic between the time of RV144 immunogen selection to the execution of the vaccine efficacy trial.Journal of virology · 2013Article
- Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes.Journal of virology · 2013Article
- Forced virus evolution reveals functional crosstalk between the disulfide bonded region and membrane proximal ectodomain region of HIV-1 gp41.Retrovirology · 2013Article
- Neutralizing antibodies to HIV-1 induced by immunization.The Journal of experimental medicine · 2013Review
- HIV-1 envelope glycoprotein resistance to monoclonal antibody 2G12 is subject-specific and context-dependent in macaques and humans.PloS one · 2013Article
- Neutralizing capacity of monoclonal antibodies that recognize peptide sequences underlying the carbohydrates on gp41 of simian immunodeficiency virus.Journal of virology · 2012Article
- Emergence of a new HIV type 1 CRF01_AE variant in Guangxi, Southern China.AIDS research and human retroviruses · 2012Article
- Kinetic mechanism for HIV-1 neutralization by antibody 2G12 entails reversible glycan binding that slows cell entry.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Neutralizing antibodies and control of HIV: moves and countermoves.Current HIV/AIDS reports · 2012Review
- Article
- Protein glycosylation in infectious disease pathobiology and treatment.Central European journal of biology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The broadly neutralizing human monoclonal antibody 2G12 binds to a carbohydrate-dependent epitope involving three major potential N-linked glycosylation sites (PNGS) of gp120 (N295, N332, and N392). Through analysis of the sensitivity to 2G12 of pseudotyped viruses carrying envelope proteins from HIV-1 clade B-infected long-term nonprogressors, we selected two naturally occurring env clones with opposite sensitivities to 2G12, albeit harboring the 3 particular PNGS known to be essential for 2G12 binding (N295, N332, and N392). The resistant clone presented a long and potentially heavily glycosylated V1V2 loop and an additional PNGS (N302) in the V3 loop. The sensitive clone harbored a short V1V2 loop and lacked the PNGS at N302. We created chimeric envelope genes by swapping the V1V2 domains of the two env clones. The influence of N302 on 2G12 sensitivity was assessed by PCR-based site-directed mutagenesis. Both the exchange of the V1V2 domain and the introduction of the PNGS at N302 on the 2G12-sensitive clone induced a significant decrease in sensitivity to 2G12. In contrast, the reverse V1V2 exchange and the removal of the PNGS at N302 on the 2G12-resistant clone increased sensitivity to 2G12, confirming the influence of these regions on 2G12 sensitivity. Our results, supported by a molecular-modeling study, suggest that both the V1V2 loop and an additional PNGS in V3 might limit access to the 2G12 epitope.
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