ArticleCell reports2013
Structural basis for enhanced HIV-1 neutralization by a dimeric immunoglobulin G form of the glycan-recognizing antibody 2G12.
Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 45 citations in OpenAlex.
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Engineered OAA lectins as selective and sensitive high mannose glycan targeting tools.bioRxiv : the preprint server for biology · 2026Article
- Article
- Unveiling the multifaceted landscape of N-glycosylation in antibody variable domains: Insights and implications.International journal of biological macromolecules · 2024Article
- i-shaped antibody engineering enables conformational tuning of biotherapeutic receptor agonists.Nature communications · 2024Article
- Avidity in antibody effector functions and biotherapeutic drug design.Nature reviews. Drug discovery · 2022Review
- Joined at the hip: The role of light chain complementarity determining region 2 in antibody self-association.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Antibody homotypic interactions are encoded by germline light chain complementarity determining region 2.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Antibody interfaces revealed through structural mining.Computational and structural biotechnology journal · 2022Article
- Strategies and Tactics for the Development of Selective Glycan-Binding Proteins.ACS chemical biology · 2021Review
- Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies.Cell · 2021Article
- HIV-1 Envelope Conformation, Allostery, and Dynamics.Viruses · 2021Review
- Antibodies for Human Immunodeficiency Virus-1 Cure Strategies.The Journal of infectious diseases · 2021Review
- Glycans in Virus-Host Interactions: A Structural Perspective.Frontiers in molecular biosciences · 2021Review
- Engineering the Human Fc Region Enables Direct Cell Killing by Cancer Glycan-Targeting Antibodies without the Need for Immune Effector Cells or Complement.Cancer research · 2020Article
- Amphiphilic Polyphenylene Dendron Conjugates for Surface Remodeling of Adenovirus 5.Angewandte Chemie (International ed. in English) · 2020Article
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- Next generation antibody drugs: pursuit of the 'high-hanging fruit'.Nature reviews. Drug discovery · 2018Review
- Article
- The role of Fc receptors in HIV prevention and therapy.Immunological reviews · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The human immunoglobulin G (IgG) 2G12 recognizes high-mannose carbohydrates on the HIV type 1 (HIV-1) envelope glycoprotein gp120. Its two antigen-binding fragments (Fabs) are intramolecularly domain exchanged, resulting in a rigid (Fab)2 unit including a third antigen-binding interface not found in antibodies with flexible Fab arms. We determined crystal structures of dimeric 2G12 IgG created by intermolecular domain exchange, which exhibits increased breadth and >50-fold increased neutralization potency compared with monomeric 2G12. The four Fab and two fragment crystalline (Fc) regions of dimeric 2G12 were localized at low resolution in two independent structures, revealing IgG dimers with two (Fab)2 arms analogous to the Fabs of conventional monomeric IgGs. Structures revealed three conformationally distinct dimers, demonstrating flexibility of the (Fab)2-Fc connections that was confirmed by electron microscopy, small-angle X-ray scattering, and binding studies. We conclude that intermolecular domain exchange, flexibility, and bivalent binding to allow avidity effects are responsible for the increased potency and breadth of dimeric 2G12.
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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.