ArticleNature communications2015
Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 137 citations in OpenAlex.
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Engineering a Coiled-Coil Protein for DARPin Presentation as a Potent SARS-CoV-2 Therapeutic.Biomacromolecules · 2025Article
- Methods for Conjugating Antibodies with Quantum Dots.Molecules (Basel, Switzerland) · 2025Review
- Glycosylation of Structured Protein Domains in Cell-Free Reaction Environments.ACS synthetic biology · 2025Article
- Modular Platform for Efficient Assembly of Multifunctional Antibodies Using Orthogonal Protein-Protein Interactions.ACS applied materials & interfaces · 2025Article
- Recent Progress in Developing Extracellular Vesicles as Nanovehicles to Deliver Carbohydrate-Based Therapeutics and Vaccines.Vaccines · 2025Review
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Isolation of full-length IgG antibodies from combinatorial libraries expressed in the cytoplasm of Escherichia coli.Nature communications · 2023Article
- Risk assessment and bioburden evaluation of Agrobacterium tumefaciens-mediated transient protein expression in plants using the CaMV35S promoter.BMC biotechnology · 2023Article
- A Novel Rabbit Anti-Myoglobin Monoclonal Antibody's Potential Application in Rhabdomyolysis Associated Acute Kidney Injury.International journal of molecular sciences · 2023Article
- Production and applications of fluorobody from redox-engineered Escherichia coli.Applied microbiology and biotechnology · 2023Article
- An Integrated In Vivo/In Vitro Protein Production Platform for Site-Specific Antibody Drug Conjugates.Bioengineering (Basel, Switzerland) · 2023Article
- Article
- A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.Nature communications · 2022Article
- Therapeutic Antibodies Against Shiga Toxins: Trends and Perspectives.Frontiers in cellular and infection microbiology · 2022Review
- Article
- Prokaryotic expression of chimeric GFP-hFc protein as a potential immune-based tool.Molecular biology research communications · 2021Article
- Enhanced Ability of Plant-Derived PGT121 Glycovariants To Eliminate HIV-1-Infected Cells.Journal of virology · 2021Article
- Expression of antibody fragments in Saccharomyces cerevisiae strains evolved for enhanced protein secretion.Microbial cell factories · 2021Article
- A useful epitope tag derived from maltose binding protein.Protein science : a publication of the Protein Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Current methods for producing immunoglobulin G (IgG) antibodies in engineered cells often require refolding steps or secretion across one or more biological membranes. Here, we describe a robust expression platform for biosynthesis of full-length IgG antibodies in the Escherichia coli cytoplasm. Synthetic heavy and light chains, both lacking canonical export signals, are expressed in specially engineered E. coli strains that permit formation of stable disulfide bonds within the cytoplasm. IgGs with clinically relevant antigen- and effector-binding activities are readily produced in the E. coli cytoplasm by grafting antigen-specific variable heavy and light domains into a cytoplasmically stable framework and remodelling the fragment crystallizable domain with amino-acid substitutions that promote binding to Fcγ receptors. The resulting cytoplasmic IgGs—named 'cyclonals'—effectively bypass the potentially rate-limiting steps of membrane translocation and glycosylation.
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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.