ReviewmAbs
IgG cooperativity - Is there allostery? Implications for antibody functions and therapeutic antibody development.
Review in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed.
- Article
- Integrative Computational Prediction Strategy for Antibody-Antigen Binding: A Case Study on Interleukin-1 Beta.Journal of chemical information and modeling · 2026Article
- Immunoglobulin-Y in Infectious Disease Diagnostics: The Ethical, Sustainability and Conditions Does It Outperform Conventional Antibodies.Infection and drug resistance · 2026Review
- New insights into antibody structure with implications for specificity, variable region restriction and isotype choice.Nature reviews. Immunology · 2025Review
- Targeted cancer treatment using a novel EGFR-specific Fc-fusion peptide based on GE11 peptide.Scientific reports · 2025Article
- Review
- Some Human Anti-Glycan Antibodies Lack the Ability to Activate the Complement System.Antibodies (Basel, Switzerland) · 2024Article
- Fc-FcγR interactions during infections: From neutralizing antibodies to antibody-dependent enhancement.Immunological reviews · 2024Review
- Identification of potential C1-binding sites in the immunoglobulin CL domains.International immunology · 2024Article
- Immunoglobulin constant regions provide stabilization to the paratope and enforce epitope specificity.The Journal of biological chemistry · 2024Article
- Monoclonal IgY antibodies: advancements and limitations for immunodiagnosis and immunotherapy applications.Therapeutic advances in vaccines and immunotherapy · 2024Review
- Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline.Biologics : targets & therapy · 2024Review
- Subclass-switched anti-spike IgG3 oligoclonal cocktails strongly enhance Fc-mediated opsonization.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- Switching Heavy Chain Constant Domains Denatures the Paratope 3D Architecture of Influenza Monoclonal Antibodies.Pathogens (Basel, Switzerland) · 2022Article
- Non-specificity as the sticky problem in therapeutic antibody development.Nature reviews. Chemistry · 2022Review
- Avidity in antibody effector functions and biotherapeutic drug design.Nature reviews. Drug discovery · 2022Review
- Non-covalent Fc-Fab interactions significantly alter internal dynamics of an IgG1 antibody.Scientific reports · 2022Article
- Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CInternational journal of molecular sciences · 2022Article
- Assessment of Functional Characterization and Comparability of Biotherapeutics: a Review.The AAPS journal · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A central dogma in immunology is that an antibody's in vivo functionality is mediated by 2 independent events: antigen binding by the variable (V) region, followed by effector activation by the constant (C) region. However, this view has recently been challenged by reports suggesting allostery exists between the 2 regions, triggered by conformational changes or configurational differences. The possibility of allosteric signals propagating through the IgG domains complicates our understanding of the antibody structure-function relationship, and challenges the current subclass selection process in therapeutic antibody design. Here we review the types of cooperativity in IgG molecules by examining evidence for and against allosteric cooperativity in both Fab and Fc domains and the characteristics of associative cooperativity in effector system activation. We investigate the origin and the mechanism of allostery with an emphasis on the C-region-mediated effects on both V and C region interactions, and discuss its implications in biological functions. While available research does not support the existence of antigen-induced conformational allosteric cooperativity in IgGs, there is substantial evidence for configurational allostery due to glycosylation and sequence variations.
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What OpenQuestion holds
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.