ArticleFrontiers in bioengineering and biotechnology2019
Factors Influencing Recombinant Protein Secretion Efficiency in Gram-Positive Bacteria: Signal Peptide and Beyond.
Article in Frontiers in bioengineering and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 65 citations in OpenAlex.
- Multi-parameter optimization of recombinant protein secretion in Bacillus subtilis: a review.Microbial cell factories · 2026Review
- UCOE-Mediated Transcriptional Stabilization Combined with EGFP-Based FACS Screening Enables Efficient Selection of High-Producing CHO Cells.Molecular biotechnology · 2026Article
- A protocol for computational design of mRNA vaccines with high functionality and specificity.Biology direct · 2026Article
- A plasmid toolbox for the easy autodisplay of recombinant proteins and its optimization.Communications biology · 2026Article
- Engineering Saccharomyces cerevisiae secretory system for recombinant protein production: strategies from signal peptides to protease control.Archives of microbiology · 2026Review
- Effect of Different Signal Peptides on the Expression of Glucoamylase fromJournal of fungi (Basel, Switzerland) · 2026Article
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Heterologous Expression and Antimicrobial Mechanism of a Cysteine-Rich Peptide from BarnacleMicroorganisms · 2025Article
- PlexinD1 is a driver and a therapeutic target in advanced prostate cancer.EMBO molecular medicine · 2025Article
- Development of high-performance inducible and secretory expression vector and host system for enhanced recombinant protein production.Scientific reports · 2024Article
- Heterologous protein exposure and secretion optimization in Mycoplasma pneumoniae.Microbial cell factories · 2024Article
- In silico design ofHeliyon · 2024Article
- Design of fully synthetic signal peptide library and its use for enhanced secretory production of recombinant proteins in Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Multiplex genetic manipulations in Clostridium butyricum and Clostridium sporogenes to secrete recombinant antigen proteins for oral-spore vaccination.Microbial cell factories · 2024Article
- Extracellular Expression of Feruloyl Esterase and Xylanase inMicroorganisms · 2023Article
- Signal Peptide Efficiency: From High-Throughput Data to Prediction and Explanation.ACS synthetic biology · 2023Article
- Modes of therapeutic delivery in synthetic microbiology.Trends in microbiology · 2023Review
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- Optimization of Signal Peptide via Site-Directed Mutagenesis for Enhanced Secretion of Heterologous Proteins inInternational journal of molecular sciences · 2022Article
- Engineered bacteria as drug delivery vehicles: Principles and prospects.Engineering microbiology · 2022Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signal peptides are short peptides directing newly synthesized proteins toward the secretory pathway. These N-terminal signal sequences are ubiquitous to all prokaryotes and eukaryotes. Signal peptides play a significant role in recombinant protein production. Previous studies have demonstrated that the secretion amount of a given target protein varies significantly depending on the signal peptide that is fused to the protein. Signal peptide selection and signal peptide modification are the two main methods for the optimization of a recombinant protein secretion. However, the highly efficient signal peptide for a target protein with a specific bacterial expression host is not predictable so far. In this article, we collect several signal peptides that have previously performed well for recombinant protein secretion in gram-positive bacteria. We also discuss several factors influencing recombinant protein secretion efficiency in gram-positive bacteria. Signal peptides with a higher charge/length ratio in n-region, more consensus residues at the-3 and-1positions in c-region and a much higher proportion of coils are more likely to perform well in the secretion of recombinant proteins. These summaries can be utilized to the selection and directed modification of signal peptides for a given recombinant protein.
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