ArticleAIDS (London, England)2010
A dimeric form of the HIV-1 antibody 2G12 elicits potent antibody-dependent cellular cytotoxicity.
Article in AIDS (London, England), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 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.
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.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Novel Compound Inhibitors of HIV-1Viruses · 2022Article
- 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
- Roles of fragment crystallizable-mediated effector functions in broadly neutralizing antibody activity against HIV.Current opinion in HIV and AIDS · 2020Review
- Understudied Factors Influencing Fc-Mediated Immune Responses against Viral Infections.Vaccines · 2019Review
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- Importance of Fc-mediated functions of anti-HIV-1 broadly neutralizing antibodies.Retrovirology · 2018Review
- Interrogation of side chain biases for oligomannose recognition by antibody 2G12 via structure-guided phage display libraries.Bioorganic & medicinal chemistry · 2017Article
- Systemic and topical use of monoclonal antibodies to prevent the sexual transmission of HIV.AIDS (London, England) · 2017Review
- Comparison of Antibody-Dependent Cell-Mediated Cytotoxicity and Virus Neutralization by HIV-1 Env-Specific Monoclonal Antibodies.Journal of virology · 2016Article
- The role of Fc receptors in HIV prevention and therapy.Immunological reviews · 2015Review
- Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy.Journal of virology · 2014Article
- Structural basis for enhanced HIV-1 neutralization by a dimeric immunoglobulin G form of the glycan-recognizing antibody 2G12.Cell reports · 2013Article
- Review
- Role of human immunodeficiency virus type 1 envelope structure in the induction of broadly neutralizing antibodies.Journal of virology · 2012Review
- Isotype modulates epitope specificity, affinity, and antiviral activities of anti-HIV-1 human broadly neutralizing 2F5 antibody.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A nonfucosylated variant of the anti-HIV-1 monoclonal antibody b12 has enhanced FcγRIIIa-mediated antiviral activity in vitro but does not improve protection against mucosal SHIV challenge in macaques.Journal of virology · 2012Article
- Candidate antibody-based therapeutics against HIV-1.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2012Review
- Neutralizing antibodies and control of HIV: moves and countermoves.Current HIV/AIDS reports · 2012Review
- A panel of IgG1 b12 variants with selectively diminished or enhanced affinity for Fcγ receptors to define the role of effector functions in protection against HIV.Journal of virology · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
objectiveIncreasing data support a role for antibody-dependent cellular cytotoxicity (ADCC) in controlling HIV-1 infection. We recently isolated a naturally occurring dimeric form of the anti-HIV-1 antibody 2G12 and found it to be significantly more potent than 2G12 monomer in neutralizing primary virus strains. However, given the unusual structure of dimeric 2G12 with two Fc regions, it was not clear whether 2G12 dimer could bind to the CD16 Fc receptor on ADCC effector cells or trigger ADCC. Here we compared the in-vitro ADCC activities of 2G12 monomer and dimer and investigated the effects of including ADCC-enhancing mutations in both forms of 2G12.
methodsAn in-vitro ADCC assay using target cells stably expressing gp160 was developed to evaluate the activities of 2G12 monomer and dimer with and without ADCC-enhancing mutations that increase the CD16-binding affinity of the 2G12 Fc region.
resultsBoth 2G12 monomer and 2G12 dimer elicited ADCC, although the dimer showed increased potency [lower half-maximal concentration (EC(50))] in triggering ADCC, thus confirming its ability to bind CD16 and trigger ADCC. The ADCC-enhancing mutations improved the ADCC activity of 2G12 monomer more than 2G12 dimer such that their EC(50) values were nearly equal. However, no increase in nonspecific ADCC activity was observed using 2G12 IgGs with these mutations.
conclusionGiven the likelihood that ADCC plays a role in protecting against initial infection and/or controlling chronic infection, these data suggest 2G12 dimers and/or addition of ADCC-enhancing mutations could augment the prophylactic and/or therapeutic potential of 2G12.
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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.