ArticleJournal of virology2011
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.
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 51 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
51 citing papers in PubMed, 62 citations in OpenAlex.
- Antiviral activity of non-neutralizing antibodies during steady-state HIV-1 infection in humanized mice.iScience · 2026Article
- Article
- Article
- Broadly neutralizing antibodies for HIV prevention: a comprehensive review and future perspectives.Clinical microbiology reviews · 2024Review
- IgG1 versus IgG3: influence of antibody-specificity and allotypic variance on virus neutralization efficacy.Frontiers in immunology · 2024Article
- Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection.Nature reviews. Immunology · 2023Review
- Mapping the interplay between NK cells and HIV: therapeutic implications.Journal of leukocyte biology · 2023Review
- Impact of structural modifications of IgG antibodies on effector functions.Frontiers in immunology · 2023Review
- Antigen-dependent modulation of immune responses to antigen-Fc fusion proteins by Fc-effector functions.Frontiers in immunology · 2023Article
- Transchromosomic bovines-derived broadly neutralizing antibodies as potent biotherapeutics to counter important emerging viral pathogens with a special focus on SARS-CoV-2, MERS-CoV, Ebola, Zika, HIV-1, and influenza A virus.Journal of medical virology · 2022Review
- Building a better antibody through the Fc: advances and challenges in harnessing antibody Fc effector functions for antiviral protection.Human vaccines & immunotherapeutics · 2021Review
- A Fc engineering approach to define functional humoral correlates of immunity against Ebola virus.Immunity · 2021Article
- Effector function does not contribute to protection from virus challenge by a highly potent HIV broadly neutralizing antibody in nonhuman primates.Science translational medicine · 2021Article
- HIV Broadly Neutralizing Antibodies Expressed as IgG3 Preserve Neutralization Potency and Show Improved Fc Effector Function.Frontiers in immunology · 2021Article
- Broadly Neutralizing Antibodies for HIV-1 Prevention.Frontiers in immunology · 2021Review
- Advancing HIV Broadly Neutralizing Antibodies: From Discovery to the Clinic.Frontiers in public health · 2021Review
- Functional Interactions of Common Allotypes of Rhesus Macaque FcγR2A and FcγR3A with Human and Macaque IgG Subclasses.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Quantifying the contribution of Fc-mediated effector functions to the antiviral activity of anti-HIV-1 IgG1 antibodies in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Tracking the Trajectory of Functional Humoral Immune Responses Following Acute HIV Infection.Frontiers in immunology · 2020Article
- Antibody-Dependent Cellular Phagocytosis in Antiviral Immune Responses.Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Passive transfer of neutralizing antibodies is effective in protecting rhesus macaques against simian/human immunodeficiency virus (SHIV) challenge. In addition to neutralization, effector functions of the crystallizable fragment (Fc) of antibodies are involved in antibody-mediated protection against a number of viruses. We recently showed that interaction between the Fc fragment of the broadly neutralizing antibody IgG1 b12 and cellular Fcγ receptors (FcγRs) plays an important role in protection against SHIV infection in rhesus macaques. The specific nature of this Fc-dependent protection is largely unknown. To investigate, we generated a panel of 11 IgG1 b12 antibody variants with selectively diminished or enhanced affinity for the two main activating FcγRs, FcγRIIa and FcγRIIIa. All 11 antibody variants bind gp120 and neutralize virus as effectively as does wild-type b12. Binding studies using monomeric (enzyme-linked immunosorbent assay [ELISA] and surface plasmon resonance [SPR]) and cellularly expressed Fcγ receptors show decreased (up to 5-fold) and increased (up to 90-fold) binding to FcγRIIa and FcγRIIIa with this newly generated panel of antibodies. In addition, there was generally a good correlation between b12 variant affinity for Fcγ receptor and variant function in antibody-dependent cell-mediated virus inhibition (ADCVI), phagocytosis, NK cell activation assays, and antibody-dependent cellular cytotoxicity (ADCC) assays. In future studies, these b12 variants will enable the investigation of the protective role of individual FcγRs in HIV infection.
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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.