ArticleCell reports2019
Affinity Maturation Enhances Antibody Specificity but Compromises Conformational Stability.
Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 100 citations in OpenAlex.
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- Epistasis and pleiotropy constrain the evolution of cross-reactive breadth in a broadly neutralizing influenza antibody.PLoS biology · 2026Article
- Aligning protein-generative models to experimental fitness with ProteinDPO.Nature methods · 2026Article
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- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Impact of heme on the therapeutic efficacy of anti-CD20 antibodies.The Journal of biological chemistry · 2026Article
- Biophysical trade-offs in antibody evolution are resolved by conformation-mediated epistasis.bioRxiv : the preprint server for biology · 2026Article
- Computational nanobody design using graph neural networks and Metropolis Monte Carlo sampling.Briefings in bioinformatics · 2026Article
- Antibody Affinity Maturation by Computational Design.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Necessity of individual VDJ-databases for annotating antibody heavy chain characteristics in non-human primates.Immunogenetics · 2025Article
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- Antibody Polyreactivity: A Challenger of Immune Paradigms.Immunology · 2025Review
- Vulnerability in the breadth evolution of an influenza broadly neutralizing antibody.bioRxiv : the preprint server for biology · 2025Article
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- Directed evolution of drug-like Aβ conformation-specific antibodies.Frontiers in immunology · 2025Article
- High-throughput specificity profiling of antibody libraries using ribosome display and microfluidics.Cell reports methods · 2024Article
- Human antibody polyreactivity is governed primarily by the heavy-chain complementarity-determining regions.Cell reports · 2024Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs) have recently emerged as one of the most promising classes of biotherapeutics. A potential advantage of B cell-derived mAbs as therapeutic agents is that they have been subjected to natural filtering mechanisms, which may enrich for B cell receptors (BCRs) with favorable biophysical properties. Here, we evaluated 400 human mAbs for polyreactivity, hydrophobicity, and thermal stability using high-throughput screening assays. Overall, mAbs derived from memory B cells and long-lived plasma cells (LLPCs) display reduced levels of polyreactivity, hydrophobicity, and thermal stability compared with naive B cell-derived mAbs. Somatic hypermutation (SHM) is inversely associated with all three biophysical properties, as well as BCR expression levels. Finally, the developability profiles of the human B cell-derived mAbs are comparable with those observed for clinical mAbs, suggesting their high therapeutic potential. The results provide insight into the biophysical consequences of affinity maturation and have implications for therapeutic antibody engineering and development.
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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.