ArticlePloS one2014
Functional production of a soluble and secreted single-chain antibody by a bacterial secretion system.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Paratope mapping of tilvestamab, an anti-AXL function-blocking antibody, using high-throughput bacterial expression of secreted scFv-osmY fusion proteins.Bioscience reports · 2025Article
- A molecular toolkit for heterologous protein secretion across Bacteroides species.Nature communications · 2024Article
- A molecular toolkit for heterologous protein secretion acrossbioRxiv : the preprint server for biology · 2023Article
- Developing a Virus-Binding Bacterium Expressing Mx Protein on the Bacterial Surface to Prevent Grouper Nervous Necrosis Virus Infection.Journal of microbiology and biotechnology · 2021Article
- Random and combinatorial mutagenesis for improved total production of secretory target protein in Escherichia coli.Scientific reports · 2021Article
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- L-Asparaginase from Erwinia carotovora: insights about its stability and activity.Molecular biology reports · 2019Article
- Accelerated directed evolution of dye-decolorizing peroxidase using a bacterial extracellular protein secretion system (BENNY).Bioresources and bioprocessing · 2019Article
- Osmotic conditions could promote scFv antibody production in theBioImpacts : BI · 2017Article
- Folding Optimization In Vivo Uncovers New Chaperones.Journal of molecular biology · 2015Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-chain variable fragments (scFvs) serve as an alternative to full-length monoclonal antibodies used in research and therapeutic and diagnostic applications. However, when recombinant scFvs are overexpressed in bacteria, they often form inclusion bodies and exhibit loss of function. To overcome this problem, we developed an scFv secretion system in which scFv was fused with osmotically inducible protein Y (osmY), a bacterial secretory carrier protein, for efficient protein secretion. Anti-EGFR scFv (αEGFR) was fused with osmY (N- and C-termini) and periplasmic leader sequence (pelB) to generate αEGFR-osmY, osmY-αEGFR, and pelB-αEGFR (control), respectively. In comparison with the control, both the osmY-fused αEGFR scFvs were soluble and secreted into the LB medium. Furthermore, the yield of soluble αEGFR-osmY was 20-fold higher, and the amount of secreted protein was 250-fold higher than that of osmY-αEGFR. In addition, the antigen-binding activity of both the osmY-fused αEGFRs was 2-fold higher than that of the refolded pelB-αEGFR from inclusion bodies. Similar results were observed with αTAG72-osmY and αHer2-osmY. These results suggest that the N-terminus of osmY fused with scFv produces a high yield of soluble, functional, and secreted scFv, and the osmY-based bacterial secretion system may be used for the large-scale industrial production of low-cost αEGFR protein.
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