ArticleThe Journal of biological chemistry2015
Fully Human VH Single Domains That Rival the Stability and Cleft Recognition of Camelid Antibodies.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Mechanistic interpretability of fine-tuned protein language models for nanobody thermostability prediction.Bioinformatics (Oxford, England) · 2026Article
- A side-by-side biophysical comparison of five single-domain antibody scaffolds used for synthetic display libraries.The Journal of biological chemistry · 2026Article
- Surface Plasmon Resonance (SPR) Workflow for Comparative Analysis of Nanobody Variants Binding to Lysozyme as a Model Ligand.Current protocols · 2026Article
- Tiny tools closing the gap: nanobodies in research and therapy.Function (Oxford, England) · 2026Review
- Novel recombinant VH43 antibody fragment potentiates the antibacterial activity of cephalosporins against Enterococcus faecium.Archives of microbiology · 2026Article
- Article
- An iterative strategy to design 4-1BB agonist nanobodies de novo with generative AI models.Scientific reports · 2025Article
- A single-domain antibody library based on a stability-engineered human VH3 scaffold.Scientific reports · 2024Article
- A VHH single-domain platform enabling discovery and development of monospecific antibodies and modular neutralizing bispecifics against SARS-CoV-2 variants.Antibody therapeutics · 2024Article
- Precision engineering for localization, validation, and modification of allergenic epitopes.The Journal of allergy and clinical immunology · 2024Review
- Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024Review
- Bringing cell therapy to tumors: considerations for optimal CAR binder design.Antibody therapeutics · 2023Review
- Characterization of an HNA aptamer suggests a non-canonical G-quadruplex motif.Nucleic acids research · 2023Article
- Inducer-free recombinant protein production in Trichoderma reesei: secretory production of endogenous enzymes and heterologous nanobodies using glucose as the sole carbon source.Microbial cell factories · 2023Article
- VSensors (Basel, Switzerland) · 2023Article
- Construction of Synthetic Antibody Phage Display Libraries.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Construction of scFv Antibodies against the Outer Loops of the MicrosporidiumInternational journal of molecular sciences · 2022Article
- Fragment-based computational design of antibodies targeting structured epitopes.Science advances · 2022Article
- The multi-specific VBritish journal of cancer · 2022Article
- Discovery of Antivirals Using Phage Display.Viruses · 2021Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human VH single domains represent a promising class of antibody fragments with applications as therapeutic modalities. Unfortunately, isolated human VH domains also generally display poor biophysical properties and a propensity to aggregate. This has encouraged the development of non-human antibody domains as alternative means of antigen recognition and, in particular, camelid (VHH) domains. Naturally devoid of light chain partners, these domains are characterized by favorable biophysical properties and propensity for cleft binding, a highly desirable characteristic, allowing the targeting of cryptic epitopes. In contrast, previously reported structures of human VH single domains had failed to recapitulate this property. Here we report the engineering and characterization of phage display libraries of stable human VH domains and the selection of binders against a diverse set of antigens. Unlike "camelized" human domains, the domains do not rely on potentially immunogenic framework mutations and maintain the structure of the VH/VL interface. Structure determination in complex with hen egg white lysozyme revealed an extended VH binding interface, with complementarity-determining region 3 deeply penetrating into the active site cleft, highly reminiscent of what has been observed for camelid domains. Taken together, our results demonstrate that fully human VH domains can be constructed that are not only stable and well expressed but also rival the cleft binding properties of camelid 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.