ArticleeLife2018
Role of framework mutations and antibody flexibility in the evolution of broadly neutralizing antibodies.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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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
60 citing papers in PubMed.
- Biophysical trade-offs in antibody evolution are resolved by conformation-mediated epistasis.bioRxiv : the preprint server for biology · 2026Article
- Antibody-antigen neutralization prediction by integrating structural information distillation and physicochemical constraints.Briefings in bioinformatics · 2026Article
- Article
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
- Structural and functional analysis of VYD222: a broadly neutralizing antibody against SARS-CoV-2 variants.bioRxiv : the preprint server for biology · 2025Article
- Optimization of a sarbecovirus llama nanobody-antigen binding interface via a combined computational and phage display protein engineering approach.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2.Nature communications · 2025Article
- Protein language model pseudolikelihoods capture features of in vivo B cell selection and evolution.Briefings in bioinformatics · 2025Article
- Protein sequence modelling with Bayesian flow networks.Nature communications · 2025Article
- Phenomenological Modeling of Antibody Response from Vaccine Strain Composition.Antibodies (Basel, Switzerland) · 2025Article
- Antibodies and cryptographic hash functions: quantifying the specificity paradox.Frontiers in immunology · 2025Article
- A paradigm shift in simulating affinity maturation to elicit broadly neutralizing antibodies.Frontiers in immunology · 2025Review
- TEMPRO: nanobody melting temperature estimation model using protein embeddings.Scientific reports · 2024Article
- Humanization of Pan-HLA-DR mAb 44H10 Hinges on Critical Residues in the Antibody Framework.Antibodies (Basel, Switzerland) · 2024Article
- Enhanced T cell receptor specificity through framework engineering.Frontiers in immunology · 2024Article
- Effects ofFrontiers in molecular biosciences · 2024Article
- Matrixed CDR grafting: A neoclassical framework for antibody humanization and developability.The Journal of biological chemistry · 2024Article
- Enhancing antibody affinity through experimental sampling of non-deleterious CDR mutations predicted by machine learning.Communications chemistry · 2023Article
- High throughput analysis of B cell dynamics and neutralizing antibody development during immunization with a novel clade C HIV-1 envelope.PLoS pathogens · 2023Article
- Arginine cluster introduction on framework region in anti-lysozyme antibody improved association rate constant by changing conformational diversity of CDR loops.Protein science : a publication of the Protein Society · 2023Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eliciting antibodies that are cross reactive with surface proteins of diverse strains of highly mutable pathogens (e.g., HIV, influenza) could be key for developing effective universal vaccines. Mutations in the framework regions of such broadly neutralizing antibodies (bnAbs) have been reported to play a role in determining their properties. We used molecular dynamics simulations and models of affinity maturation to study specific bnAbs against HIV. Our results suggest that there are different classes of evolutionary lineages for the bnAbs. If germline B cells that initiate affinity maturation have high affinity for the conserved residues of the targeted epitope, framework mutations increase antibody rigidity as affinity maturation progresses to evolve bnAbs. If the germline B cells exhibit weak/moderate affinity for conserved residues, an initial increase in flexibility via framework mutations may be required for the evolution of bnAbs. Subsequent mutations that increase rigidity result in highly potent bnAbs. Implications of our results for immunogen design are discussed.
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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.