ArticleMicrobial cell factories2020
Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region.
Article in Microbial cell factories, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- High-cell-density Escherichia coli-based nanobody production: benchmarking of subcellular targeting, strain background and process development strategies.Microbial cell factories · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Outer Membrane Vesicles as a Versatile Platform for Vaccine Development: Engineering Strategies, Applications and Challenges.Journal of extracellular vesicles · 2025Review
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Recent advances in recombinant production of soluble proteins in E. coli.Microbial cell factories · 2025Review
- A bacteriocin expression platform for targeting pathogenic bacterial species.Nature communications · 2024Article
- Biosensor that Detects Stress Caused by Periplasmic Proteins.ACS synthetic biology · 2024Article
- Protein Expression and Purification of Romiplostim and Analysis of Its Secretory Production Using anReports of biochemistry & molecular biology · 2023Article
- Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.MicrobiologyOpen · 2023Article
- Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.Microbial cell factories · 2022Review
- Current trends in biopharmaceuticals production in Escherichia coli.Biotechnology letters · 2022Review
- Antibiotic-Efficient Genetic Cassette for the TEM-1 β-Lactamase That Improves Plasmid Performance.ACS synthetic biology · 2022Article
- Signal amplification ofSynthetic biology (Oxford, England) · 2022Article
- Implementing Novel Designs in pET Expression Plasmids that Increase Protein Production.Bio-protocol · 2021Article
- Random and combinatorial mutagenesis for improved total production of secretory target protein in Escherichia coli.Scientific reports · 2021Article
- Improved production of Humira antibody in the genetically engineered Escherichia coli SHuffle, by co-expression of human PDI-GPx7 fusions.Applied microbiology and biotechnology · 2020Article
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8 authors.
Funding
Abstract
backgroundRecombinant proteins are often engineered with an N-terminal signal peptide, which facilitates their secretion to the oxidising environment of the periplasm (gram-negative bacteria) or the culture supernatant (gram-positive bacteria). A commonly encountered problem is that the signal peptide influences the synthesis and secretion of the recombinant protein in an unpredictable manner. A molecular understanding of this phenomenon is highly sought after, as it could lead to improved methods for producing recombinant proteins in bacterial cell factories.
resultsHerein we demonstrate that signal peptides contribute to an unpredictable translation initiation region. A directed evolution approach that selects a new translation initiation region, whilst leaving the amino acid sequence of the signal peptide unchanged, can increase production levels of secreted recombinant proteins. The approach can increase production of single chain antibody fragments, hormones and other recombinant proteins in the periplasm of E. coli.
conclusionsThe study demonstrates that signal peptide performance is coupled to the efficiency of the translation initiation region.
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