ArticlemAbs2016
Assessing kinetic and epitopic diversity across orthogonal monoclonal antibody generation platforms.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- Trends in industrialization and commercialization of IgY technology.Frontiers in immunology · 2022Review
- Highly Potent Immunotoxins Targeting the Membrane-distal N-lobe of GPC3 for Immunotherapy of Hepatocellular Carcinoma.Journal of Cancer · 2022Article
- Humanization of Chicken-Derived Antibodies by Yeast Surface Display.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Accelerated antibody discovery targeting the SARS-CoV-2 spike protein for COVID-19 therapeutic potential.Antibody therapeutics · 2021Article
- Anti-GD2 antibody dinutuximab inhibits triple-negative breast tumor growth by targeting GD2Journal for immunotherapy of cancer · 2021Article
- Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021Article
- Localization of the Interaction Site of Herpes Simplex Virus Glycoprotein D (gD) on the Membrane Fusion Regulator, gH/gL.Journal of virology · 2020Article
- Characterizing Epitope Binding Regions of Entire Antibody Panels by Combining Experimental and Computational Analysis of Antibody: Antigen Binding Competition.Molecules (Basel, Switzerland) · 2020Article
- Hybridoma technology a versatile method for isolation of monoclonal antibodies, its applicability across species, limitations, advancement and future perspectives.International immunopharmacology · 2020Review
- Kinetic Exclusion Assay of Biomolecules by Aptamer Capture.Sensors (Basel, Switzerland) · 2020Article
- Epitope-directed antibody selection by site-specific photocrosslinking.Science advances · 2020Article
- Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies.Molecular therapy. Methods & clinical development · 2020Article
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- Surface Plasmon Resonance Reveals Direct Binding of Herpes Simplex Virus Glycoproteins gH/gL to gD and Locates a gH/gL Binding Site on gD.Journal of virology · 2019Article
- Surrogate potency assays: Comparison of binding profiles complements dose response curves for unambiguous assessment of relative potencies.Journal of pharmaceutical analysis · 2018Article
- Strategies for Generating Diverse Antibody Repertoires Using Transgenic Animals Expressing Human Antibodies.Frontiers in immunology · 2018Article
- Increased breadth of HIV-1 neutralization achieved by diverse antibody clones each with limited neutralization breadth.PloS one · 2018Article
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- Global sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.PLoS pathogens · 2017Article
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Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability of monoclonal antibodies (mAbs) to target specific antigens with high precision has led to an increasing demand to generate them for therapeutic use in many disease areas. Historically, the discovery of therapeutic mAbs has relied upon the immunization of mammals and various in vitro display technologies. While the routine immunization of rodents yields clones that are stable in serum and have been selected against vast arrays of endogenous, non-target self-antigens, it is often difficult to obtain species cross-reactive mAbs owing to the generally high sequence similarity shared across human antigens and their mammalian orthologs. In vitro display technologies bypass this limitation, but lack an in vivo screening mechanism, and thus may potentially generate mAbs with undesirable binding specificity and stability issues. Chicken immunization is emerging as an attractive mAb discovery method because it combines the benefits of both in vivo and in vitro display methods. Since chickens are phylogenetically separated from mammals, their proteins share less sequence homology with those of humans, so human proteins are often immunogenic and can readily elicit rodent cross-reactive clones, which are necessary for in vivo proof of mechanism studies. Here, we compare the binding characteristics of mAbs isolated from chicken immunization, mouse immunization, and phage display of human antibody libraries. Our results show that chicken-derived mAbs not only recapitulate the kinetic diversity of mAbs sourced from other methods, but appear to offer an expanded repertoire of epitopes. Further, chicken-derived mAbs can bind their native serum antigen with very high affinity, highlighting their therapeutic potential.
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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.