ArticleSpringerPlus2016
OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system.
Article in SpringerPlus, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
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- Production of Xylooligosaccharides (XOSs) with Anti-inflammatory and Prebiotic Activities Using Recombinant Endo-1,4-β-xylanases fromJournal of agricultural and food chemistry · 2026Article
- A modular biodevice assembly tool kit for combinatorial screening and benchmarking multiple cell surface display platforms in Escherichia coli.Journal of biological engineering · 2026Article
- Engineering PET surface colonization with a synthetic bacterial consortium.Frontiers in bioengineering and biotechnology · 2026Article
- Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- Comparative Secretory Efficiency of Two Chitosanase Signal Peptides from Bacillus subtilis in Escherichia coli.Journal of microbiology (Seoul, Korea) · 2024Article
- Engineered E. coli Nissle 1917 for delivery of bioactive IL-2 for cancer immunotherapy.Scientific reports · 2023Article
- Protein Expression and Purification of Romiplostim and Analysis of Its Secretory Production Using anReports of biochemistry & molecular biology · 2023Article
- Deep Antimicrobial Activity and Stability Analysis Inform Lysin Sequence-Function Mapping.ACS synthetic biology · 2023Article
- An outlook to sophisticated technologies and novel developments for metabolic regulation in theFrontiers in bioengineering and biotechnology · 2023Review
- In silico and in vitro analysis of a rational mutation in gIII signal peptide and its effects on periplasmic expression of rhGH in E. coli.Archives of microbiology · 2022Article
- Highly Expressed Soluble Recombinant Anti-GFP VHHs inFrontiers in molecular biosciences · 2022Article
- Soluble versions of outer membrane cytochromes function as exporters for heterologously produced cargo proteins.Microbial cell factories · 2019Article
- Engineering the flagellar type III secretion system: improving capacity for secretion of recombinant protein.Microbial cell factories · 2019Article
- Efficient production of human zona pellucida-3 in a prokaryotic expression system.World journal of microbiology & biotechnology · 2018Article
- Secretion of recombinant proteins fromEngineering in life sciences · 2018Review
- Efficient extracellular recombinant production and purification of a Bacillus cyclodextrin glucanotransferase in Escherichia coli.Microbial cell factories · 2017Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The production of secreted recombinant proteins from E. coli is pivotal to the biotechnological industry because it reduces the cost of downstream processing. Proteins destined for secretion contain an N-terminal signal peptide that is cleaved by secretion machinery in the plasma membrane. The resulting protein is released in an active mature form. In this study, Bacillus subtilis chitosanase (Csn) was used as a model protein to compare the effect of two signal peptides on the secretion of heterologous recombinant protein. The results showed that the E. coli secretion machinery could recognize both native bacillus and E. coli signal peptides. However, only the native bacillus signal peptide could generate the same N-terminal sequence as in the wild type bacteria. When the recombinant Csn constructs contained the E. coli OmpA signal peptide, the secreted enzymes were heterogeneous, comprising a mixed population of secreted enzymes with different N-terminal sequences. Nevertheless, the E. coli OmpA signal peptide was found to be more efficient for high expression and secretion of bacillus Csn. These findings may be used to help engineer other recombinant proteins for secretory production in E. coli.
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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.