ArticlemAbs2016
High affinity nanobodies against human epidermal growth factor receptor selected on cells by E. coli display.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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
15 citing papers in PubMed, 38 citations in OpenAlex.
- Plant-Produced Viral Nanoparticles Decorated with Nanobodies Against HER2 Improve Retention and Recruitment of Immune Cells in Solid Tumors.Advanced healthcare materials · 2026Article
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- A nanobody-based therapeutic targeting Nipah virus limits viral escape.Nature structural & molecular biology · 2025Article
- High-throughput strategies for monoclonal antibody screening: advances and challenges.Journal of biological engineering · 2025Review
- Improving the production and stability of nanobodies.Protein engineering, design & selection : PEDS · 2025Article
- Bacterial surface display of human lectins in Escherichia coli.Microbial biotechnology · 2024Article
- NANOBODIES®: A Review of Diagnostic and Therapeutic ApplicationsInternational journal of molecular sciences · 2023Review
- Flow cytometric evaluation of yeast-bacterial cell-cell interactions.Biotechnology and bioengineering · 2023Article
- Synthetic biology: at the crossroads of genetic engineering and human therapeutics-a Keystone Symposia report.Annals of the New York Academy of Sciences · 2021Review
- Nanobodies for Medical Imaging: About Ready for Prime Time?Biomolecules · 2021Review
- Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody.Scientific reports · 2021Article
- Nanobodies targeting immune checkpoint molecules for tumor immunotherapy and immunoimaging (Review).International journal of molecular medicine · 2021Review
- BeQuIK (Biosensor Engineered Quorum Induced Killing): designer bacteria for destroying recalcitrant biofilms.Microbial biotechnology · 2020Article
- Single-Domain Antibodies and the Promise of Modular Targeting in Cancer Imaging and Treatment.Frontiers in immunology · 2018Review
- Escherichia coli surface display for the selection of nanobodies.Microbial biotechnology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most therapeutic antibodies (Abs) target cell surface proteins on tumor and immune cells. Cloning of Ab gene libraries in E. coli and their display on bacteriophages is commonly used to select novel therapeutic Abs binding target antigens, either purified or expressed on cells. However, the sticky nature of bacteriophages renders phage display selections on cells challenging. We previously reported an E. coli display system for expression of VHHs (i.e., nanobodies, Nbs) on the surface of bacteria and selection of high-affinity clones by magnetic cell sorting (MACS). Here, we demonstrate that E. coli display is also an attractive method for isolation of Nbs against cell surface antigens, such as the epidermal growth factor receptor (EGFR), upon direct selection and screening of Ab libraries on live cells. We employ a whole cell-based strategy using a VHH library obtained by immunization with human tumor cells over-expressing EGFR (i.e., A431), and selection of bacterial clones bound to murine fibroblast NIH-3T3 cells transfected with human EGFR, after depletion of non-specific clones on untransfected cells. This strategy resulted in the isolation of high-affinity Nbs binding distinct epitopes of EGFR, including Nbs competing with the ligand, EGF, as characterized by flow cytometry of bacteria displaying the Nbs and binding assays with purified Nbs using surface plasmon resonance. Hence, our study demonstrates that E. coli display of VHH libraries and selection on cells enables efficient isolation and characterization of high-affinity Nbs against cell surface antigens.
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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.