ArticleBioconjugate chemistry2021
Dual Site-Specific Chemoenzymatic Antibody Fragment Conjugation Using CRISPR-Based Hybridoma Engineering.
Article in Bioconjugate chemistry, 2021. 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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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Quantitative Proteomics and CRISPR/Cas9 Editing Reveal UPR-Mediated Control of Immunoglobulin Homeostasis in Hybridomas.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Sortase A Catalyzed Transpeptidation for Protein Bioengineering.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Homogeneous antibody-drug conjugates with dual payloads: potential, methods and considerations.mAbs · 2025Review
- Cancer Antibody Engineering: Comparison of Mammalian, Yeast, Bacterial, Plants, Cell-free and Hybridoma Expression Systems.Current pharmaceutical biotechnology · 2025Review
- Homogeneous multi-payload antibody-drug conjugates.Nature chemistry · 2024Review
- Sortase-mediated labeling: Expanding frontiers in site-specific protein functionalization opens new research avenues.Current opinion in chemical biology · 2024Review
- Episomal Vectors for Stable Production of Recombinant Proteins and Engineered Antibodies.Antibodies (Basel, Switzerland) · 2024Article
- Antibody-drug conjugates in cancer therapy: innovations, challenges, and future directions.Archives of pharmacal research · 2024Review
- Pfs230 Domain 7 is targeted by a potent malaria transmission-blocking monoclonal antibody.NPJ vaccines · 2023Article
- CRISPR/Cas9-based Engineering of Immunoglobulin Loci in Hybridoma Cells.Bio-protocol · 2023Article
- Combined Application of Orthogonal Sortases and Depsipeptide Substrates for Dual Protein Labeling.Bioconjugate chemistry · 2022Article
- Substantially Improved Electrofusion Efficiency of Hybridoma Cells: Based on the Combination of Nanosecond and Microsecond Pulses.Bioengineering (Basel, Switzerland) · 2022Article
- Antibody dual-functionalisation enabled through a modular divinylpyrimidine disulfide rebridging strategy.Chemical communications (Cambridge, England) · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Antibody-drug conjugates for the treatment of lymphoma: clinical advances and latest progress.Journal of hematology & oncology · 2021Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functionalized antibodies and antibody fragments have found applications in the fields of biomedical imaging, theranostics, and antibody-drug conjugates (ADC). In addition, therapeutic and theranostic approaches benefit from the possibility to deliver more than one type of cargo to target cells, further challenging stochastic labeling strategies. Thus, bioconjugation methods to reproducibly obtain defined homogeneous conjugates bearing multiple different cargo molecules, without compromising target affinity, are in demand. Here, we describe a straightforward CRISPR/Cas9-based strategy to rapidly engineer hybridoma cells to secrete Fab' fragments bearing two distinct site-specific labeling motifs, which can be separately modified by two different sortase A mutants. We show that sequential genetic editing of the heavy chain (HC) and light chain (LC) loci enables the generation of a stable cell line that secretes a dual tagged Fab' molecule (DTFab'), which can be easily isolated. To demonstrate feasibility, we functionalized the DTFab' with two distinct cargos in a site-specific manner. This technology platform will be valuable in the development of multimodal imaging agents, theranostics, and next-generation ADCs.
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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.