ArticlemAbs
Bivalent binding on cells varies between anti-CD20 antibodies and is dose-dependent.
Article in mAbs. 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.
- SSTR2 receptor states and cellular metabolism modulateEANM innovation · 2026Article
- Molecular basis of CXC chemokine receptor 3 ligand multispecificity.Science advances · 2026Article
- Pharmacokinetic profiling of rituximab in glomerular diseases: key determinants and implications for personalized therapy.Frontiers in pharmacology · 2026Review
- Severe anaphylactic shock reaction upon rituximab rechallenge in membranous nephropathy: a case report and literature review.Frontiers in pharmacology · 2026Article
- Understanding antibody-target antigen interactions and the avidity effect using mathematical modelling.Journal of the Royal Society, Interface · 2025Article
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- Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8.Nature communications · 2023Article
- Parameter estimation and identifiability analysis for a bivalent analyte model of monoclonal antibody-antigen binding.Analytical biochemistry · 2023Article
- Update on the Application of Monoclonal Antibody Therapy in Primary Membranous Nephropathy.Drugs · 2023Review
- Article
- Physiological Considerations for ModelingFrontiers in pharmacology · 2022Review
- The selection of variable regions affects effector mechanisms of IgA antibodies against CD20.Blood advances · 2021Article
- KEuropean biophysics journal : EBJ · 2021Article
- Targeting B Cells to Modify MS, NMOSD, and MOGAD: Part 1.Neurology(R) neuroimmunology & neuroinflammation · 2021Review
- Complement Activation in the Treatment of B-Cell Malignancies.Antibodies (Basel, Switzerland) · 2020Review
- Complement-Dependent Activity of CD20-Specific IgG Correlates With Bivalent Antigen Binding and C1q Binding Strength.Frontiers in immunology · 2020Article
- Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on their mechanism of action, two types of anti-CD20 antibodies are distinguished: Type I, which efficiently mediate complement-dependent cytotoxicity, and Type II, which instead are more efficient in inducing direct cell death. Several molecular characteristics of these antibodies have been suggested to underlie these different biological functions, one of these being the manner of binding to CD20 expressed on malignant B cells. However, the exact binding model on cells is unclear. In this study, the binding mechanism of the Type I therapeutic antibodies rituximab (RTX) and ofatumumab (OFA) and the Type II antibody obinutuzumab (OBI) were established by real-time interaction analysis on live cells. It was found that the degree of bivalent stabilization differed for the antibodies: OFA was stabilized the most, followed by RTX and then OBI, which had the least amount of bivalent stabilization. Bivalency inversely correlated with binding dynamics for the antibodies, with OBI displaying the most dynamic binding pattern, followed by RTX and OFA. For RTX and OBI, bivalency and binding dynamics were concentration dependent; at higher concentrations the interactions were more dynamic, whereas the percentage of antibodies that bound bivalent was less, resulting in concentration-dependent apparent affinities. This was barely noticeable for OFA, as almost all molecules bound bivalently at the tested concentrations. We conclude that the degree of bivalent binding positively correlates with the complement recruiting capacity of the investigated CD20 antibodies.
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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.