ArticleWorld journal of microbiology & biotechnology2014
Co-expression of Dsb proteins enables soluble expression of a single-chain variable fragment (scFv) against human type 1 insulin-like growth factor receptor (IGF-1R) in E. coli.
Article in World journal of microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 2026Article
- Evolution ofInternational journal of molecular sciences · 2020Review
- Construction of an expression vector mediated by the dual promoter for prokaryotic and mammalian cell expression system.Molecular biology reports · 2020Article
- Tuning recombinant protein expression to match secretion capacity.Microbial cell factories · 2018Article
- Efficient treatment of Parkinson's disease using ultrasonography-guided rhFGF20 proteoliposomes.Drug delivery · 2018Article
- Development an effective system to expression recombinant protein in E. coli via comparison and optimization of signal peptides: Expression of Pseudomonas fluorescens BJ-10 thermostable lipase as case study.Microbial cell factories · 2018Article
- Effects of Environmental Factors on Soluble Expression of a Humanized Anti-TNF-α scFv Antibody in Escherichia coli.Advanced pharmaceutical bulletin · 2015Article
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3 authors at 1 institution in 1 country.
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Abstract
Type 1 insulin-like growth factor receptor (IGF-1R) is a promising therapeutic target for cancer treatment. A single-chain variable fragment (scFv) against human IGF-1R forms inclusion body when expressed in periplasmic space of E. coli routinely. Here, we described that co-expression of appropriate disulfide bonds (Dsb) proteins known to catalyze the formation and isomerization of Dsb can markedly recover the soluble expression of target scFv in E. coli. A 50 % recovery in solubility of the scFv was observed upon co-expression of DsbC alone, and a maximum solubility (80 %) was obtained when DsbA and DsbC were co-expressed in combination. Furthermore, the soluble scFv present full antigen-binding activity with IGF-1R, suggesting its correct folding. This study also suggested that the selection of Dsb proteins should be tested case-by-case if the approach of co-expression of Dsb system is adopted to address the problem of insoluble expression of proteins carrying Dsb.
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